› 3iw3

X-ray diffraction
1.8Å resolution

Crystal structure of hyperthermophilic nitrilase

Released:
DOI: 10.2210/pdb3iw3/pdb
PDB entry 3iw3 coloured by chain, front view.
PDB entry 3iw3 coloured by chain, side view.
PDB entry 3iw3 coloured by chain, top view.
Source organism: Pyrococcus abyssi GE5
Primary publication:
Crystallographic analysis of a thermoactive nitrilase.
Raczynska JE, Vorgias CE, Antranikian G, Rypniewski W
J Struct Biol 173 294-302 (2011)
PMID: 21095228

Function and Biology Details

Reaction catalysed: 
A nitrile + 2 H(2)O = a carboxylate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194136 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitrilase Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 29.79 KDa
Source organism: Pyrococcus abyssi GE5
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UYV8 (Residues: 1-262; Coverage: 100%)
Gene names: PAB1449, PYRAB13990
Sequence domains: Carbon-nitrogen hydrolase
Structure domains: Carbon-nitrogen hydrolase

Ligands and Environments

2 bound ligands:
Ligand ACY 3 x ACY
Ligand MG 1 x MG
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P41
Unit cell:
a: 59.162Å b: 59.162Å c: 128.975Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.159 0.206
Expression system: Escherichia coli

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Citations

2 review citations

Nitrile-converting enzymes as a tool to improve biocatalysis in organic synthesis: recent insights and promises.
Gong et al. (2017)
1 more

1 mention without citation

Functional metagenomics uncovers nitrile-hydrolysing enzymes in a coal metagenome.
Achudhan et al. (2023)