› 2w1v

X-ray diffraction
1.49Å resolution

Crystal structure of mouse nitrilase-2 at 1.4A resolution

Released:
DOI: 10.2210/pdb2w1v/pdb
PDB entry 2w1v coloured by chain, front view.
PDB entry 2w1v coloured by chain, side view.
PDB entry 2w1v coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Functional proteomic and structural insights into molecular recognition in the nitrilase family enzymes.
Barglow KT, Saikatendu KS, Bracey MH, Huey R, Morris GM, Olson AJ, Stevens RC, Cravatt BF
Biochemistry 47 13514-23 (2008)
PMID: 19053248

Function and Biology Details

Reaction catalysed: 
A monoamide of a dicarboxylate + H(2)O = a dicarboxylate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191598 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Omega-amidase NIT2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 276 amino acids
Theoretical weight: 30.54 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9JHW2 (Residues: 1-276; Coverage: 100%)
Gene names: D16Ertd502e, Nit2
Sequence domains: Carbon-nitrogen hydrolase
Structure domains: Carbon-nitrogen hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P32
Unit cell:
a: 90.268Å b: 90.268Å c: 54.059Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.144 0.142 0.177
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Covalent protein modification: the current landscape of residue-specific electrophiles.
Shannon et al. (2015)
6 more

10 mentions without citation

Fast and anisotropic flexibility-rigidity index for protein flexibility and fluctuation analysis.
Opron et al. (2014)
9 more