1ire: Difference between revisions
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<StructureSection load='1ire' size='340' side='right'caption='[[1ire]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1ire' size='340' side='right'caption='[[1ire]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ire]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ire]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19285 Atcc 19285]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IRE FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitrile_hydratase Nitrile hydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.84 4.2.1.84] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ire FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ire OCA], [https://pdbe.org/1ire PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ire RCSB], [https://www.ebi.ac.uk/pdbsum/1ire PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ire ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/NHAA_PSETH NHAA_PSETH]] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. [[https://www.uniprot.org/uniprot/NHAB_PSETH NHAB_PSETH]] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 10:13, 14 April 2021
Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophilaCrystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila
Structural highlights
Function[NHAA_PSETH] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. [NHAB_PSETH] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of cobalt-containing nitrile hydratase from Pseudonocardia thermophila JCM 3095 at 1.8 A resolution revealed the structure of the noncorrin cobalt at the catalytic center. Two cysteine residues (alphaCys(111) and alphaCys(113)) coordinated to the cobalt were posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively, like in iron-containing nitrile hydratase. A tryptophan residue (betaTrp(72)), which may be involved in substrate binding, replaced the tyrosine residue of iron-containing nitrile hydratase. The difference seems to be responsible for the preference for aromatic nitriles rather than aliphatic ones of cobalt-containing nitrile hydratase. Crystal structure of cobalt-containing nitrile hydratase.,Miyanaga A, Fushinobu S, Ito K, Wakagi T Biochem Biophys Res Commun. 2001 Nov 16;288(5):1169-74. PMID:11700034[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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