Structure of PDB 3vyh Chain A

Receptor sequence
>3vyhA (length=203) Species: 1848 (Pseudonocardia thermophila) [Search protein sequence]
TENILRKSDEEIQKEITARVKALESMLIEQGILTTSMIDRMAEIYENEVG
PHLGAKVVVKAWTDPEFKKRLLADGTEACKELGIGGLQGEDMMWVENTDE
VHHVVVCTLCSCYPRPVLGLPPNWFKEPQYRSRVVREPRQLLKEEFGFEV
PPSKEIKVWDSSSEMRFVVLPQRPAGTDGWSEEELATLVTRESMIGVEPA
KAV
3D structure
PDB3vyh Effects of argnine residue around the substrate pocket on the substrate specificity of thiocyanate hydrolase
ChainA
Resolution1.63 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C108 C111 S112 C113
Catalytic site (residue number reindexed from 1) C107 C110 S111 C112
Enzyme Commision number 4.2.1.84: nitrile hydratase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CO A C108 A111 S112 C113 C107 A110 S111 C112
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0018822 nitrile hydratase activity
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
GO:0050897 cobalt ion binding
GO:0080109 indole-3-acetonitrile nitrile hydratase activity
Biological Process
GO:0050899 nitrile catabolic process
Cellular Component
GO:0005575 cellular_component

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3vyh, PDBe:3vyh, PDBj:3vyh
PDBsum3vyh
PubMed
UniProtQ7SID2|NHAA_PSETH Cobalt-containing nitrile hydratase subunit alpha

[Back to BioLiP]