Structure of PDB 1ahj Chain G

Receptor sequence
>1ahjG (length=198) Species: 76275 (Rhodococcus sp. R312) [Search protein sequence]
ENAAPAQAAVSDRAWALFRALDGKGLVPDGYVEGWKKTFEEDFSPRRGAE
LVARAWTDPEFRQLLLTDGTAAVAQYGYLGPQGEYIVAVEDTPTLKNVIV
CSLCSCTAWPILGLPPTWYKSFEYRARVVREPRKVLSEMGTEIASDIEIR
VYDTTAETRYMVLPQRPAGTEGWSQEQLQEIVTKDCLIGVAIPQVPTV
3D structure
PDB1ahj Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold.
ChainG
Resolution2.65 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) 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 G C110 C113 S114 C115 C101 C104 S105 C106
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:1ahj, PDBe:1ahj, PDBj:1ahj
PDBsum1ahj
PubMed9195885
UniProtP13448|NHAA_RHOER Nitrile hydratase subunit alpha (Gene Name=nthA)

[Back to BioLiP]