2sec - Revision history

OCA at 09:23, 21 February 2024

2024-02-21T09:23:50Z

← Older revision		Revision as of 09:23, 21 February 2024
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	<StructureSection load='2sec' size='340' side='right'caption='[[2sec]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2sec' size='340' side='right'caption='[[2sec]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898~~] and [https://en.wikipedia.org/wiki/~~Hirme Hirme~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2SEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2SEC FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.8Å</td></tr>
	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]~~ </~~span~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2sec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sec OCA], [https://pdbe.org/2sec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2sec RCSB], [https://www.ebi.ac.uk/pdbsum/2sec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2sec ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2sec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sec OCA], [https://pdbe.org/2sec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2sec RCSB], [https://www.ebi.ac.uk/pdbsum/2sec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2sec ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/~~SUBT_BACLI SUBT_BACLI]~~] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. ~~[[https~~:~~//www~~.~~uniprot~~.~~org~~/~~uniprot~~/~~ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.~~		[https://www.uniprot.org/uniprot/SUBC_BACLI SUBC_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).<ref>PMID:11109488</ref> <ref>PMID:4967581</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2sec ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2sec ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The crystal structures of the molecular complexes between two serine proteinases and two of their protein inhibitors have been determined: subtilisin Carlsberg with the recombinant form of eglin-c from the leech Hirudo medicinalis and subtilisin Novo with chymotrypsin inhibitor 2 from barley seeds. The structures have been fully refined by restrained-parameter least-squares methods to crystallographic R factors (sigma[[Fo[ - [Fc[[/sigma[Fo[) of 0.136 at 1.8-A resolution and 0.154 at 2.1-A resolution, respectively. The 274 equivalent alpha-carbon atoms of the enzymes superpose with an rms deviation of 0.53 A. Sequence changes between the enzymes result in localized structural adjustments. Functional groups in the active sites superpose with an rms deviation of 0.19 A for 161 equivalent atoms; this close similarity in the conformation of active-site residues provides no obvious reason for known differences in catalytic activity between Carlsberg and Novo. Conformational changes in the active-site region indicate a small induced fit of enzyme and inhibitor. Some conformational differences are observed between equivalent active-site residues of subtilisin Carlsberg and alpha-chymotrypsin. Despite differences in tertiary architecture, most enzyme-substrate (inhibitor) interactions are maintained. Subtilisin Carlsberg has a rare cis-peptide bond preceding Thr211 (Gly211 in Novo). Both enzymes contain tightly bound Ca2+ ions. Site 1 is heptacoordinate with the oxygen atoms at the vertices of a pentagonal bipyramid. Site 2 in Carlsberg is probably occupied by a K+ ion in Novo. Conserved water molecules appear to play important structural roles in the enzyme interior, in the inhibitor beta-sheet, and at the enzyme-inhibitor interface. The 62 equivalent alpha-carbon atoms of the inhibitors superpose with an rms deviation of 1.68 A. Sequence changes result in somewhat different packing of the alpha-helix, beta-sheet, and reactive-site loop relative to each other. Hydrogen bonds and electrostatic interactions supporting the conformation of the reactive-site loop are conserved. The 24 main-chain plus C beta atoms of P4 to P1' overlap with an rms deviation of 0.19 A. Features contributing to the inhibitory nature of eglin-c and CI-2 are discussed.

	Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo.,McPhalen CA, James MN Biochemistry. 1988 Aug 23;27(17):6582-98. PMID:3064813<ref>PMID:3064813</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2sec" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Clostridium licheniforme weigmann 1898~~]]		[[Category: Bacillus licheniformis]]
	[[Category: ~~Hirme~~]]		[[Category: Hirudo medicinalis]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Subtilisin]]~~		[[Category: James MNG]]
	[[Category: James~~, M N.G~~]]		[[Category: Mcphalen CA]]
	[[Category: Mcphalen~~, C A~~]]

OCA at 20:54, 20 October 2021

2021-10-20T20:54:55Z

← Older revision		Revision as of 20:54, 20 October 2021
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	<StructureSection load='2sec' size='340' side='right'caption='[[2sec]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2sec' size='340' side='right'caption='[[2sec]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898] and [~~http~~://en.wikipedia.org/wiki/Hirme Hirme]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2SEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898] and [https://en.wikipedia.org/wiki/Hirme Hirme]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2SEC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2sec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sec OCA], [~~http~~://pdbe.org/2sec PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2sec RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2sec PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2sec ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2sec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sec OCA], [https://pdbe.org/2sec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2sec RCSB], [https://www.ebi.ac.uk/pdbsum/2sec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2sec ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/SUBT_BACLI SUBT_BACLI]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. [[~~http~~://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.		[[https://www.uniprot.org/uniprot/SUBT_BACLI SUBT_BACLI]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. [[https://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Eglin\|Eglin]]		*[[Eglin\|Eglin]]
	*[[Subtilisin\|Subtilisin]]		*[[Subtilisin 3D structures\|Subtilisin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:02, 18 December 2019

2019-12-18T14:02:46Z

← Older revision		Revision as of 14:02, 18 December 2019
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	==STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO==		==STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO==
	<StructureSection load='2sec' size='340' side='right' caption='[[2sec]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2sec' size='340' side='right'caption='[[2sec]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898] and [http://en.wikipedia.org/wiki/Hirme Hirme]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898] and [http://en.wikipedia.org/wiki/Hirme Hirme]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SEC FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/se/2sec_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/se/2sec_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 2sec" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2sec" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Eglin\|Eglin]]
			*[[Subtilisin\|Subtilisin]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Clostridium licheniforme weigmann 1898]]		[[Category: Clostridium licheniforme weigmann 1898]]
	[[Category: Hirme]]		[[Category: Hirme]]
			[[Category: Large Structures]]
	[[Category: Subtilisin]]		[[Category: Subtilisin]]
	[[Category: James, M N.G]]		[[Category: James, M N.G]]
	[[Category: Mcphalen, C A]]		[[Category: Mcphalen, C A]]

OCA at 07:11, 29 November 2017

2017-11-29T07:11:51Z

← Older revision		Revision as of 07:11, 29 November 2017
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 2sec" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2sec" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Eglin\|Eglin]]
	*[[Subtilisin\|Subtilisin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:51, 5 August 2016

2016-08-05T14:51:15Z

← Older revision		Revision as of 14:51, 5 August 2016
Line 1:		Line 1:

	==STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO==		==STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO==
	<StructureSection load='2sec' size='340' side='right' caption='[[2sec]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2sec' size='340' side='right' caption='[[2sec]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_licheniformis Bacillus licheniformis~~] and [http://en.wikipedia.org/wiki/~~Hirudo_medicinalis Hirudo medicinalis~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898] and [http://en.wikipedia.org/wiki/Hirme Hirme]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SEC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2sec RCSB], [http://www.ebi.ac.uk/pdbsum/2sec PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sec OCA], [http://pdbe.org/2sec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2sec RCSB], [http://www.ebi.ac.uk/pdbsum/2sec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2sec ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2sec ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2sec" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacillus licheniformis~~]]		[[Category: Clostridium licheniforme weigmann 1898]]
	[[Category: ~~Hirudo medicinalis~~]]		[[Category: Hirme]]
	[[Category: Subtilisin]]		[[Category: Subtilisin]]
	[[Category: James, M N.G]]		[[Category: James, M N.G]]
	[[Category: Mcphalen, C A]]		[[Category: Mcphalen, C A]]

OCA at 19:43, 25 December 2014

2014-12-25T19:43:00Z

← Older revision		Revision as of 19:43, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SEC FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2sec RCSB], [http://www.ebi.ac.uk/pdbsum/2sec PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2sec RCSB], [http://www.ebi.ac.uk/pdbsum/2sec PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/SUBT_BACLI SUBT_BACLI]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. [[http://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Hirudo medicinalis]]		[[Category: Hirudo medicinalis]]
	[[Category: Subtilisin]]		[[Category: Subtilisin]]
	[[Category: James, M N.G.]]		[[Category: James, M N.G]]
	[[Category: Mcphalen, C A.]]		[[Category: Mcphalen, C A]]

OCA at 07:47, 29 September 2014

2014-09-29T07:47:09Z

← Older revision		Revision as of 07:47, 29 September 2014
Line 1:		Line 1:
	[[Image:~~2sec~~.~~png~~\|~~left~~\|~~200px~~]]		==STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO==
			<StructureSection load='2sec' size='340' side='right' caption='[[2sec]], [[Resolution\|resolution]] 1.80Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2sec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SEC FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2sec RCSB], [http://www.ebi.ac.uk/pdbsum/2sec PDBsum]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/se/2sec_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The crystal structures of the molecular complexes between two serine proteinases and two of their protein inhibitors have been determined: subtilisin Carlsberg with the recombinant form of eglin-c from the leech Hirudo medicinalis and subtilisin Novo with chymotrypsin inhibitor 2 from barley seeds. The structures have been fully refined by restrained-parameter least-squares methods to crystallographic R factors (sigma[[Fo[ - [Fc[[/sigma[Fo[) of 0.136 at 1.8-A resolution and 0.154 at 2.1-A resolution, respectively. The 274 equivalent alpha-carbon atoms of the enzymes superpose with an rms deviation of 0.53 A. Sequence changes between the enzymes result in localized structural adjustments. Functional groups in the active sites superpose with an rms deviation of 0.19 A for 161 equivalent atoms; this close similarity in the conformation of active-site residues provides no obvious reason for known differences in catalytic activity between Carlsberg and Novo. Conformational changes in the active-site region indicate a small induced fit of enzyme and inhibitor. Some conformational differences are observed between equivalent active-site residues of subtilisin Carlsberg and alpha-chymotrypsin. Despite differences in tertiary architecture, most enzyme-substrate (inhibitor) interactions are maintained. Subtilisin Carlsberg has a rare cis-peptide bond preceding Thr211 (Gly211 in Novo). Both enzymes contain tightly bound Ca2+ ions. Site 1 is heptacoordinate with the oxygen atoms at the vertices of a pentagonal bipyramid. Site 2 in Carlsberg is probably occupied by a K+ ion in Novo. Conserved water molecules appear to play important structural roles in the enzyme interior, in the inhibitor beta-sheet, and at the enzyme-inhibitor interface. The 62 equivalent alpha-carbon atoms of the inhibitors superpose with an rms deviation of 1.68 A. Sequence changes result in somewhat different packing of the alpha-helix, beta-sheet, and reactive-site loop relative to each other. Hydrogen bonds and electrostatic interactions supporting the conformation of the reactive-site loop are conserved. The 24 main-chain plus C beta atoms of P4 to P1' overlap with an rms deviation of 0.19 A. Features contributing to the inhibitory nature of eglin-c and CI-2 are discussed.

	~~{{STRUCTURE_2sec\| PDB=2sec \| SCENE= }}~~		Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo.,McPhalen CA, James MN Biochemistry. 1988 Aug 23;27(17):6582-98. PMID:3064813<ref>PMID:3064813</ref>

	~~===STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_3064813}}~~

	~~==About this Structure==~~
	~~[[2sec]] is~~ a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. This structure supersedes the ~~now removed PDB entry [http://oca~~.~~weizmann~~.ac.~~il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA].~~

	==See Also==		==See Also==
	*[[Eglin\|Eglin]]		*[[Eglin\|Eglin]]
	*[[Subtilisin\|Subtilisin]]		*[[Subtilisin\|Subtilisin]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:003064813<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Bacillus licheniformis]]		[[Category: Bacillus licheniformis]]
	[[Category: Hirudo medicinalis]]		[[Category: Hirudo medicinalis]]

OCA at 20:41, 20 October 2012

2012-10-20T20:41:16Z

← Older revision		Revision as of 20:41, 20 October 2012
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	==About this Structure==		==About this Structure==
	[[2sec]] is a 2 chain structure ~~of [[Eglin]] and [[Subtilisin]]~~ with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA].		[[2sec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sec 1sec]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SEC OCA].

	==See Also==		==See Also==
Line 15:		Line 15:

	==Reference==		==Reference==
	<ref group="xtra">PMID:003064813~~</ref><ref group="xtra">PMID:007770448~~</ref><references group="xtra"/>		<ref group="xtra">PMID:003064813</ref><references group="xtra"/>
	[[Category: Bacillus licheniformis]]		[[Category: Bacillus licheniformis]]
	[[Category: Hirudo medicinalis]]		[[Category: Hirudo medicinalis]]

OCA at 11:17, 27 July 2012

2012-07-27T11:17:54Z

← Older revision		Revision as of 11:17, 27 July 2012
Line 1:		Line 1:
	[[Image:2sec.png\|left\|200px]]		[[Image:2sec.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2sec", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2sec\| PDB=2sec \| SCENE= }}		{{STRUCTURE_2sec\| PDB=2sec \| SCENE= }}

	===STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO===		===STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_3064813}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 3064813 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_3064813}}		{{ABSTRACT_PUBMED_3064813}}

Line 22:		Line 11:

	==See Also==		==See Also==
	*[[Eglin]]		*[[Eglin\|Eglin]]
	*[[Subtilisin]]		*[[Subtilisin\|Subtilisin]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~3064813~~</ref><references group="xtra"/>		<ref group="xtra">PMID:003064813</ref><ref group="xtra">PMID:007770448</ref><references group="xtra"/>
	[[Category: Bacillus licheniformis]]		[[Category: Bacillus licheniformis]]
	[[Category: Hirudo medicinalis]]		[[Category: Hirudo medicinalis]]

OCA: Protected "2sec" [edit=sysop:move=sysop]

2010-12-26T20:08:11Z

Protected "2sec" [edit=sysop:move=sysop]

← Older revision	Revision as of 20:08, 26 December 2010
(No difference)