1v29: Difference between revisions
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|PDB= 1v29 |SIZE=350|CAPTION= <scene name='initialview01'>1v29</scene>, resolution 2.6Å | |PDB= 1v29 |SIZE=350|CAPTION= <scene name='initialview01'>1v29</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CO:COBALT (II) ION'>CO</scene> | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ahj|1AHJ]], [[2ahj|2AHJ]], [[1ire|1IRE]] | |||
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1v29 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v29 RCSB]</span> | |||
}} | }} | ||
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[[Category: Takashima, Y.]] | [[Category: Takashima, Y.]] | ||
[[Category: Yanagi, K.]] | [[Category: Yanagi, K.]] | ||
[[Category: bacillus smithii]] | [[Category: bacillus smithii]] | ||
[[Category: nhase]] | [[Category: nhase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:18:25 2008'' | ||
Revision as of 00:18, 31 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | |||||||
| Activity: | Nitrile hydratase, with EC number 4.2.1.84 | ||||||
| Related: | 1AHJ, 2AHJ, 1IRE
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Nitrile hydratase from a thermophile Bacillus smithii
OverviewOverview
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.
About this StructureAbout this Structure
1V29 is a Protein complex structure of sequences from Bacillus smithii. Full crystallographic information is available from OCA.
ReferenceReference
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
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