› 1kp0

X-ray diffraction
2.7Å resolution

The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus

Released:
DOI: 10.2210/pdb1kp0/pdb
PDB entry 1kp0 coloured by chain, front view.
PDB entry 1kp0 coloured by chain, side view.
PDB entry 1kp0 coloured by chain, top view.
Source organism: Actinobacillus
Primary publication:
Structure of creatine amidinohydrolase from Actinobacillus.
Padmanabhan B, Paehler A, Horikoshi M
Acta Crystallogr D Biol Crystallogr 58 1322-8 (2002)
PMID: 12136144

Function and Biology Details

Reaction catalysed: 
Creatine + H(2)O = 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-181943 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 402 amino acids
Theoretical weight: 44.73 KDa
Source organism: Actinobacillus
UniProt:
  • Canonical: Q7SIB5 (Residues: 1-402; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: I222
Unit cell:
a: 111.263Å b: 113.624Å c: 191.649Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.222

Quick links

Citations

1 review citation

The Origin and Evolution of Release Factors: Implications for Translation Termination, Ribosome Rescue, and Quality Control Pathways.
Burroughs et al. (2019)
2 other articles

2 mentions without citation

The structural basis of ATP as an allosteric modulator.
Lu et al. (2014)
1 more