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| | <StructureSection load='1v29' size='340' side='right'caption='[[1v29]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1v29' size='340' side='right'caption='[[1v29]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1v29]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_smithii Bacillus smithii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V29 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v29]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_smithii Bacillus smithii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V29 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ahj|1ahj]], [[2ahj|2ahj]], [[1ire|1ire]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrile_hydratase Nitrile hydratase], with EC number [http://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'>[https://proteopedia.org/fgij/fg.htm?mol=1v29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v29 OCA], [https://pdbe.org/1v29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v29 RCSB], [https://www.ebi.ac.uk/pdbsum/1v29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v29 ProSAT]</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=1v29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v29 OCA], [http://pdbe.org/1v29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v29 RCSB], [http://www.ebi.ac.uk/pdbsum/1v29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v29 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q84FS5_9BACI Q84FS5_9BACI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Bacillus smithii]] | | [[Category: Bacillus smithii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nitrile hydratase]]
| + | [[Category: Hourai S]] |
| - | [[Category: Hourai, S]] | + | [[Category: Miki M]] |
| - | [[Category: Miki, M]] | + | [[Category: Mitsuda S]] |
| - | [[Category: Mitsuda, S]] | + | [[Category: Takashima Y]] |
| - | [[Category: Takashima, Y]] | + | [[Category: Yanagi K]] |
| - | [[Category: Yanagi, K]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Nhase]]
| + | |
| Structural highlights
Function
Q84FS5_9BACI
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 PubMed
The crystal structure of the nitrile hydratase (NHase) from Bacillus smithii SC-J05-1 was determined. Our analysis of the structure shows that some residues that seem to be responsible for substrate recognition are different from those of other NHases. In particular, the Phe52 in the beta subunit of NHase from B. smithii covers the metal center partially like a small lid and narrows the active site cleft. It is well known that the NHase from B. smithii especially prefers aliphatic nitriles for its substrate rather than aromatic ones, and we can now infer that the Phe52 residue may play a key role in the substrate specificity for this enzyme. This finding leads us to suggest that substitution of these residues may alter the substrate specificity of the enzyme.
Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii.,Hourai S, Miki M, Takashima Y, Mitsuda S, Yanagi K Biochem Biophys Res Commun. 2003 Dec 12;312(2):340-5. PMID:14637142[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hourai S, Miki M, Takashima Y, Mitsuda S, Yanagi K. Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii. Biochem Biophys Res Commun. 2003 Dec 12;312(2):340-5. PMID:14637142
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