X-ray diffraction
1.8Å resolution

Structure and a Proposed Mechanism for Ornithine Cyclodeaminase from Pseudomonas putida


Function and Biology Details

Reaction catalysed:
L-ornithine = L-proline + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Ornithine cyclodeaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 350 amino acids
Theoretical weight: 38.85 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
  • Canonical: Q88H32 (Residues: 1-350; Coverage: 100%)
Gene names: PP_3533, ocd
Sequence domains: Ornithine cyclodeaminase/mu-crystallin family
Structure domains:

Ligands and Environments

Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 69.9Å b: 78.6Å c: 119.9Å
α: 90° β: 90° γ: 90°
R R work R free
0.158 0.158 0.181
Expression system: Escherichia coli