› 3a6h

X-ray diffraction
2Å resolution

Function and Biology Details

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

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: 260 amino acids
Theoretical weight: 28.48 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P83772 (Residues: 1-260; Coverage: 100%)
Gene name: crnA
Sequence domains: Creatinine amidohydrolase
Structure domains: Creatininase

Ligands and Environments

3 bound ligands:
Ligand MN 6 x MN
Ligand ZN 6 x ZN
Ligand CL 6 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 106.8Å b: 60.24Å c: 146.2Å
α: 90° β: 100.3° γ: 90°
R-values:
R R work R free
0.199 0.199 0.231
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Metabolism and distribution of pharmacological homoarginine in plasma and main organs of the anesthetized rat.
Günes et al. (2017)
2 more