› 1q3k

X-ray diffraction
2.1Å resolution

Crystal structure of creatinine amidohydrolase (creatininase)

Released:
DOI: 10.2210/pdb1q3k/pdb
PDB entry 1q3k coloured by chain, front view.
PDB entry 1q3k coloured by chain, side view.
PDB entry 1q3k coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Crystal structure of creatininase from Pseudomonas putida: a novel fold and a case of convergent evolution.
Beuth B, Niefind K, Schomburg D
J Mol Biol 332 287-301 (2003)
PMID: 12946365

Function and Biology Details

Reaction catalysed: 
Creatinine + H(2)O = creatine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160738 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Creatinine amidohydrolase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 259 amino acids
Theoretical weight: 28.43 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P83772 (Residues: 2-260; Coverage: 100%)
Gene name: crnA
Sequence domains: Creatinine amidohydrolase
Structure domains: Creatininase

Ligands and Environments

2 bound ligands:
Ligand ZN 12 x ZN
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P21
Unit cell:
a: 74.392Å b: 94.084Å c: 114.746Å
α: 90° β: 104.62° γ: 90°
R-values:
R R work R free
0.209 0.207 0.247
Expression system: Escherichia coli

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Citations

7 citation in other articles

The crystal structure of a novel, latent dihydroorotase from Aquifex aeolicus at 1.7A resolution.
Martin et al. (2005)
6 more