› 1j2u

X-ray diffraction
1.85Å resolution

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: 260 amino acids
Theoretical weight: 28.6 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

2 bound ligands:
Ligand ZN 12 x ZN
Ligand SO4 10 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P212121
Unit cell:
a: 102.114Å b: 151.449Å c: 167.633Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.201
Expression system: Escherichia coli

Quick links

Citations

1 review citation

[Biochemistry and structural biology of microbial enzymes and their medical applications].
Yoshimoto T. (2007)
11 other articles

1 mention without citation

The Creatininase Homolog MftE from Mycobacterium smegmatis Catalyzes a Peptide Cleavage Reaction in the Biosynthesis of a Novel Ribosomally Synthesized Post-translationally Modified Peptide (RiPP).
Bruender et al. (2017)