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==Crystal structure of 1-pyrroline-4-hydroxy-2-carboxylate deaminase from Brucella melitensis with covalently bound substrate==
==Crystal structure of 1-pyrroline-4-hydroxy-2-carboxylate deaminase from Brucella melitensis with covalently bound substrate==
<StructureSection load='4o0k' size='340' side='right' caption='[[4o0k]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='4o0k' size='340' side='right'caption='[[4o0k]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4o0k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brumb Brumb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O0K FirstGlance]. <br>
<table><tr><td colspan='2'>[[4o0k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_melitensis_ATCC_23457 Brucella melitensis ATCC 23457]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O0K FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</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=4o0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0k OCA], [https://pdbe.org/4o0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o0k RCSB], [https://www.ebi.ac.uk/pdbsum/4o0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0k ProSAT]</span></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mpq|4mpq]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMEA_B0240 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=546272 BRUMB])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1-pyrroline-4-hydroxy-2-carboxylate_deaminase 1-pyrroline-4-hydroxy-2-carboxylate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.22 3.5.4.22] </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=4o0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0k OCA], [http://pdbe.org/4o0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o0k RCSB], [http://www.ebi.ac.uk/pdbsum/4o0k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C0RKH4_BRUMB C0RKH4_BRUMB]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 1-pyrroline-4-hydroxy-2-carboxylate deaminase]]
[[Category: Brucella melitensis ATCC 23457]]
[[Category: Brumb]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Brucella melitensis]]
[[Category: Lyase]]
[[Category: Pyruvate]]
[[Category: Ssgcid]]

Revision as of 08:50, 18 January 2023

Crystal structure of 1-pyrroline-4-hydroxy-2-carboxylate deaminase from Brucella melitensis with covalently bound substrate

4o0k, resolution 1.50Å

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