Structure of PDB 2qdy Chain A

Receptor sequence
>2qdyA (length=197) Species: 1833 (Rhodococcus erythropolis) [Search protein sequence]
ENAAPAQAPVSDRAWALFRALDGKGLVPDGYVEGWKKTFEEDFSPRRGAE
LVARAWTDPEFRQLLLTDGTAAVAQYGYLGPQGEYIVAVEDTPTLKNVIV
CSLCSCTAWPILGLPPTWYKSFEYRARVVREPRKVLSEMGTEIASDIEIR
VYDTTAETRYMVLPQRPAGTEGWSQEQLQEIVTKDCLIGVAIPQVPT
3D structure
PDB2qdy High resolution X-ray molecular structure of the nitrile hydratase from Rhodococcus erythropolis AJ270 reveals posttranslational oxidation of two cysteines into sulfinic acids and a novel biocatalytic nitrile hydration mechanism
ChainA
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C110 C113 S114 C115
Catalytic site (residue number reindexed from 1) C101 C104 S105 C106
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 FE A C110 A113 S114 A115 C101 A104 S105 A106
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0018822 nitrile hydratase activity
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
GO:0080109 indole-3-acetonitrile nitrile hydratase activity

View graph for
Molecular Function
External links
PDB RCSB:2qdy, PDBe:2qdy, PDBj:2qdy
PDBsum2qdy
PubMed17716629
UniProtP13448|NHAA_RHOER Nitrile hydratase subunit alpha (Gene Name=nthA)

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