› 1v7z

X-ray diffraction
1.6Å 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 sp.
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

4 bound ligands:
Ligand MN 6 x MN
Ligand ZN 6 x ZN
Ligand SO4 18 x SO4
Ligand CRN 6 x CRN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 102.186Å b: 152.211Å c: 167.119Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.198
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

1 mention without citation

Self-association of a highly charged arginine-rich cell-penetrating peptide.
Tesei et al. (2017)