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2oof
From Proteopedia
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<StructureSection load='2oof' size='340' side='right'caption='[[2oof]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2oof' size='340' side='right'caption='[[2oof]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2oof]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2oof]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OOF FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2oof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oof OCA], [https://pdbe.org/2oof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oof RCSB], [https://www.ebi.ac.uk/pdbsum/2oof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oof ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2oof TOPSAN]</span></td></tr> | |
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HUTI_AERHH HUTI_AERHH] Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.[HAMAP-Rule:MF_00372] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Imidazolonepropionase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Unidentified]] |
| - | [[Category: Burley | + | [[Category: Burley SK]] |
| - | [[Category: Eswaramoorthy | + | [[Category: Eswaramoorthy S]] |
| - | + | [[Category: Swaminathan S]] | |
| - | [[Category: Swaminathan | + | [[Category: Tyagi R]] |
| - | [[Category: Tyagi | + | |
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Current revision
The crystal structure of 4-imidazolone-5-propanoate amidohydrolase from environmental sample
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