1mod - Revision history

OCA at 06:40, 13 August 2026

2026-08-13T06:40:15Z

← Older revision		Revision as of 06:40, 13 August 2026
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mod_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mod_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<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/main_output.php?pdb_ID=1mod 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=1mod ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The highly conserved distal histidine residue (His64) of sperm whale myoglobin modulates the affinity of ligands. In an effort to fully characterize the effects of mutating residue 64, we have determined the high-resolution crystal structures of the Gly64, Val64, Leu64, Thr64 and Gln64 mutants in several liganded forms. Metmyoglobins with hydrophobic substitutions at residue 64 (Val64 and Leu64) lack a water molecule at the sixth coordination position, while those with polar amino acid residues at this position (wild-type and Gln64) retain a covalently bound water molecule. In the Thr64 mutant, the bound water position is only partially occupied. In contrast, mutating the distal histidine residue to glycine does not cause loss of the coordinated water molecule, because the hydrogen bond from the imidazole side-chain is replaced by one from a well-ordered solvent water molecule. Differences in water structure around the distal pocket are apparent also in the structures of deoxymyoglobin mutants. The water molecule that is hydrogen-bonded to the N epsilon atom of histidine 64 in wild-type deoxymyoglobin is not found in any of the position 64 mutant structures that were determined. Comparison of the carbonmonoxy structures of wild-type, Gly64, Leu64 and Gln64 myoglobins in the P6 crystal form shows that the conformation of the Fe-C-O complex is nearly linear and is independent of the identity of the amino acid residue at position 64. However, the effect of CO binding on the conformation of residue 64 is striking. Superposition of deoxy and carbonmonoxy structures reveals significant displacements of the residue 64 side-chain in the wild-type and Gln64 myoglobins, but no displacement in the Leu64 mutant. These detailed structural studies provide key insights into the mechanisms of ligand binding and discrimination in myoglobin.

			High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin.,Quillin ML, Arduini RM, Olson JS, Phillips GN Jr J Mol Biol. 1993 Nov 5;234(1):140-55. PMID:8230194<ref>PMID:8230194</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 1mod" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Myoglobin 3D structures\|Myoglobin 3D structures]]		*[[Myoglobin 3D structures\|Myoglobin 3D structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:46, 14 February 2024

2024-02-14T07:46:35Z

← Older revision		Revision as of 07:46, 14 February 2024
Line 3:		Line 3:
	<StructureSection load='1mod' size='340' side='right'caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1mod' size='340' side='right'caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Phycd Phycd~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [https://pdbe.org/1mod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [https://www.ebi.ac.uk/pdbsum/1mod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mod 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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [https://pdbe.org/1mod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [https://www.ebi.ac.uk/pdbsum/1mod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mod ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.		[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 20:
	</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=1mod 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=1mod ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The highly conserved distal histidine residue (His64) of sperm whale myoglobin modulates the affinity of ligands. In an effort to fully characterize the effects of mutating residue 64, we have determined the high-resolution crystal structures of the Gly64, Val64, Leu64, Thr64 and Gln64 mutants in several liganded forms. Metmyoglobins with hydrophobic substitutions at residue 64 (Val64 and Leu64) lack a water molecule at the sixth coordination position, while those with polar amino acid residues at this position (wild-type and Gln64) retain a covalently bound water molecule. In the Thr64 mutant, the bound water position is only partially occupied. In contrast, mutating the distal histidine residue to glycine does not cause loss of the coordinated water molecule, because the hydrogen bond from the imidazole side-chain is replaced by one from a well-ordered solvent water molecule. Differences in water structure around the distal pocket are apparent also in the structures of deoxymyoglobin mutants. The water molecule that is hydrogen-bonded to the N epsilon atom of histidine 64 in wild-type deoxymyoglobin is not found in any of the position 64 mutant structures that were determined. Comparison of the carbonmonoxy structures of wild-type, Gly64, Leu64 and Gln64 myoglobins in the P6 crystal form shows that the conformation of the Fe-C-O complex is nearly linear and is independent of the identity of the amino acid residue at position 64. However, the effect of CO binding on the conformation of residue 64 is striking. Superposition of deoxy and carbonmonoxy structures reveals significant displacements of the residue 64 side-chain in the wild-type and Gln64 myoglobins, but no displacement in the Leu64 mutant. These detailed structural studies provide key insights into the mechanisms of ligand binding and discrimination in myoglobin.

	High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin.,Quillin ML, Arduini RM, Olson JS, Phillips GN Jr J Mol Biol. 1993 Nov 5;234(1):140-55. PMID:8230194<ref>PMID:8230194</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 1mod" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Myoglobin 3D structures\|Myoglobin 3D structures]]		*[[Myoglobin 3D structures\|Myoglobin 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Phycd~~]]		[[Category: Physeter catodon]]
	[[Category: Phillips~~, G N~~]]		[[Category: Phillips Jr GN]]
	[[Category: Quillin~~, M L]]~~		[[Category: Quillin ML]]
	~~[[Category: Oxygen storage~~]]

OCA at 09:28, 5 May 2021

2021-05-05T09:28:39Z

← Older revision		Revision as of 09:28, 5 May 2021
Line 3:		Line 3:
	<StructureSection load='1mod' size='340' side='right'caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1mod' size='340' side='right'caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1MOD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [~~http~~://pdbe.org/1mod PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1mod PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1mod 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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [https://pdbe.org/1mod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [https://www.ebi.ac.uk/pdbsum/1mod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mod ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.		[[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:

	==See Also==		==See Also==
	*[[Myoglobin\|Myoglobin]]		*[[Myoglobin 3D structures\|Myoglobin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:17, 31 July 2019

2019-07-31T07:17:53Z

← Older revision		Revision as of 07:17, 31 July 2019
Line 1:		Line 1:

	==HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN==		==HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN==
	<StructureSection load='1mod' size='340' side='right' caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1mod' size='340' side='right'caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOD FirstGlance]. <br>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mod_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mod_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 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1mod" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1mod" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Myoglobin\|Myoglobin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Phycd]]		[[Category: Phycd]]
	[[Category: Phillips, G N]]		[[Category: Phillips, G N]]
	[[Category: Quillin, M L]]		[[Category: Quillin, M L]]
	[[Category: Oxygen storage]]		[[Category: Oxygen storage]]

OCA at 10:07, 25 October 2017

2017-10-25T10:07:57Z

← Older revision		Revision as of 10:07, 25 October 2017
Line 1:		Line 1:

	==HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN==		==HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN==
	<StructureSection load='1mod' size='340' side='right' caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1mod' size='340' side='right' caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [http://pdbe.org/1mod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [http://www.ebi.ac.uk/pdbsum/1mod 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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [http://pdbe.org/1mod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [http://www.ebi.ac.uk/pdbsum/1mod PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mod ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	<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=1mod 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:
	</div>		</div>
	<div class="pdbe-citations 1mod" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1mod" style="background-color:#fffaf0;"></div>

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

OCA at 08:14, 11 September 2015

2015-09-11T08:14:08Z

← Older revision		Revision as of 08:14, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1mod' size='340' side='right' caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1mod' size='340' side='right' caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Physeter_catodon Physeter catodon~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [http://www.ebi.ac.uk/pdbsum/1mod 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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [http://pdbe.org/1mod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [http://www.ebi.ac.uk/pdbsum/1mod PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 1mod" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Physeter catodon~~]]		[[Category: Phycd]]
	[[Category: Phillips, G N]]		[[Category: Phillips, G N]]
	[[Category: Quillin, M L]]		[[Category: Quillin, M L]]
	[[Category: Oxygen storage]]		[[Category: Oxygen storage]]

OCA at 13:43, 25 December 2014

2014-12-25T13:43:05Z

← Older revision		Revision as of 13:43, 25 December 2014
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOD FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [http://www.ebi.ac.uk/pdbsum/1mod 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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [http://www.ebi.ac.uk/pdbsum/1mod PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Physeter catodon]]		[[Category: Physeter catodon]]
	[[Category: Phillips, G N.]]		[[Category: Phillips, G N]]
	[[Category: Quillin, M L.]]		[[Category: Quillin, M L]]
	[[Category: Oxygen storage]]		[[Category: Oxygen storage]]

OCA at 15:55, 28 September 2014

2014-09-28T15:55:00Z

← Older revision		Revision as of 15:55, 28 September 2014
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	[[Image:~~1mod~~.~~png~~\|~~left~~\|~~200px~~]]		==HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN==
			<StructureSection load='1mod' size='340' side='right' caption='[[1mod]], [[Resolution\|resolution]] 2.00Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOD FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
			<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=1mod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mod RCSB], [http://www.ebi.ac.uk/pdbsum/1mod 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/mo/1mod_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 highly conserved distal histidine residue (His64) of sperm whale myoglobin modulates the affinity of ligands. In an effort to fully characterize the effects of mutating residue 64, we have determined the high-resolution crystal structures of the Gly64, Val64, Leu64, Thr64 and Gln64 mutants in several liganded forms. Metmyoglobins with hydrophobic substitutions at residue 64 (Val64 and Leu64) lack a water molecule at the sixth coordination position, while those with polar amino acid residues at this position (wild-type and Gln64) retain a covalently bound water molecule. In the Thr64 mutant, the bound water position is only partially occupied. In contrast, mutating the distal histidine residue to glycine does not cause loss of the coordinated water molecule, because the hydrogen bond from the imidazole side-chain is replaced by one from a well-ordered solvent water molecule. Differences in water structure around the distal pocket are apparent also in the structures of deoxymyoglobin mutants. The water molecule that is hydrogen-bonded to the N epsilon atom of histidine 64 in wild-type deoxymyoglobin is not found in any of the position 64 mutant structures that were determined. Comparison of the carbonmonoxy structures of wild-type, Gly64, Leu64 and Gln64 myoglobins in the P6 crystal form shows that the conformation of the Fe-C-O complex is nearly linear and is independent of the identity of the amino acid residue at position 64. However, the effect of CO binding on the conformation of residue 64 is striking. Superposition of deoxy and carbonmonoxy structures reveals significant displacements of the residue 64 side-chain in the wild-type and Gln64 myoglobins, but no displacement in the Leu64 mutant. These detailed structural studies provide key insights into the mechanisms of ligand binding and discrimination in myoglobin.

	~~{{STRUCTURE_1mod\| PDB=1mod \| SCENE= }}~~		High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin.,Quillin ML, Arduini RM, Olson JS, Phillips GN Jr J Mol Biol. 1993 Nov 5;234(1):140-55. PMID:8230194<ref>PMID:8230194</ref>

	~~===HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_8230194}}~~

	~~==About this Structure==~~
	~~[[1mod]] is~~ a ~~1 chain structure with sequence from [http://en.wikipedia~~.~~org/wiki/Physeter_catodon Physeter catodon]~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann.ac.il/oca-bin~~/~~ocashort?id=1MOD OCA].~~

	==See Also==		==See Also==
	*[[Myoglobin\|Myoglobin]]		*[[Myoglobin\|Myoglobin]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:008230194<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Physeter catodon]]		[[Category: Physeter catodon]]
	[[Category: Phillips, G N.]]		[[Category: Phillips, G N.]]
	[[Category: Quillin, M L.]]		[[Category: Quillin, M L.]]
	[[Category: Oxygen storage]]		[[Category: Oxygen storage]]

OCA at 17:22, 20 October 2012

2012-10-20T17:22:59Z

← Older revision		Revision as of 17:22, 20 October 2012
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	==About this Structure==		==About this Structure==
	[[1mod]] is a 1 chain structure ~~of [[Myoglobin]]~~ with sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA].		[[1mod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOD OCA].

	==See Also==		==See Also==

OCA at 00:43, 27 July 2012

2012-07-27T00:43:32Z

← Older revision		Revision as of 00:43, 27 July 2012
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	[[Image:1mod.png\|left\|200px]]		[[Image:1mod.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_1mod", 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_1mod\| PDB=1mod \| SCENE= }}		{{STRUCTURE_1mod\| PDB=1mod \| SCENE= }}

	===HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN===		===HIGH-RESOLUTION CRYSTAL STRUCTURES OF DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_8230194}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 8230194 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_8230194}}		{{ABSTRACT_PUBMED_8230194}}

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	==See Also==		==See Also==
	*[[Myoglobin]]		*[[Myoglobin\|Myoglobin]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~8230194~~</ref><references group="xtra"/>		<ref group="xtra">PMID:008230194</ref><references group="xtra"/>
	[[Category: Physeter catodon]]		[[Category: Physeter catodon]]
	[[Category: Phillips, G N.]]		[[Category: Phillips, G N.]]
	[[Category: Quillin, M L.]]		[[Category: Quillin, M L.]]
	[[Category: Oxygen storage]]		[[Category: Oxygen storage]]