Structure of PDB 1ugs Chain A

Receptor sequence
>1ugsA (length=203) Species: 1848 (Pseudonocardia thermophila) [Search protein sequence]
TENILRKSDEEIQKEITARVKALESMLIEQGILTTSMIDRMAEIYENEVG
PHLGAKVVVKAWTDPEFKKRLLADGTEACKELGIGGLQGEDMMWVENTDE
VHHVVVCTLCSCTPWPVLGLPPNWFKEPQYRSRVVREPRQLLKEEFGFEV
PPSKEIKVWDSSSEMRFVVLPQRPAGTDGWSEEELATLVTRESMIGVEPA
KAV
3D structure
PDB1ugs Mutational and structural analysis of cobalt-containing nitrile hydratase on substrate and metal binding
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 C111 S112 C113 C107 C110 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ugs, PDBe:1ugs, PDBj:1ugs
PDBsum1ugs
PubMed14717710
UniProtQ7SID2|NHAA_PSETH Cobalt-containing nitrile hydratase subunit alpha

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