› 3qz5

X-ray diffraction
2.5Å resolution

Crystal Structure of Co-type Nitrile Hydratase alpha-E168Q from Pseudomonas putida.

Released:
DOI: 10.2210/pdb3qz5/pdb
PDB entry 3qz5 coloured by chain, front view.
PDB entry 3qz5 coloured by chain, side view.
PDB entry 3qz5 coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Evidence of the participation of remote residues in the catalytic activity of Co-type nitrile hydratase from Pseudomonas putida.
Brodkin HR, Novak WR, Milne AC, D'Aquino JA, Karabacak NM, Goldberg IG, Agar JN, Payne MS, Petsko GA, Ondrechen MJ, Ringe D
Biochemistry 50 4923-35 (2011)
PMID: 21473592

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163957 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Co-type Nitrile Hydratase alpha subunit Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 211 amino acids
Theoretical weight: 23.14 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21(DE3)
Structure domains: Nitrile hydratase alpha /Thiocyanate hydrolase gamma
Co-type Nitrile Hydratase beta subunit Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 219 amino acids
Theoretical weight: 24.05 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21(DE3)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 4 x GOL
Ligand 3CO 4 x 3CO
1 modified residue:
Ligand CSD 8 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 82.526Å b: 137.975Å c: 85.321Å
α: 90° β: 91.97° γ: 90°
R-values:
R R work R free
0.21 0.208 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Electric Fields and Enzyme Catalysis.
Fried et al. (2017)
2 more

2 mentions without citation

Evidence of the participation of remote residues in the catalytic activity of Co-type nitrile hydratase from Pseudomonas putida.
Brodkin et al. (2011)
1 more