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› 1chm

X-ray diffraction
1.9Å resolution

ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES

Released:
DOI: 10.2210/pdb1chm/pdb
PDB entry 1chm coloured by chain, front view.
PDB entry 1chm coloured by chain, side view.
PDB entry 1chm coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures.
Coll M, Knof SH, Ohga Y, Messerschmidt A, Huber R, Moellering H, Rüssmann L, Schumacher G
J Mol Biol 214 597-610 (1990)
PMID: 1696320

Function and Biology Details

Reaction catalysed: 
creatine + H2O = sarcosine + urea.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153656 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Creatinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 401 amino acids
Theoretical weight: 45.33 KDa
Source organism: Pseudomonas putida
Expression system: Not provided
UniProt:
  • Canonical: P38488 (Residues: 2-402; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CMS 2 x CMS
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 60.83Å b: 110.55Å c: 62.63Å
α: 90° β: 102.22° γ: 90°
R-values:
R R work R free
0.177 0.177 not available
Expression system: Not provided

Quick links

Citations

5 review citations

Creatine and creatinine metabolism.
Wyss et al. (2000)
4 more

6 mentions without citation

The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module.
Stuwe et al. (2008)
5 more