› 1akm

X-ray diffraction
2.8Å resolution

ORNITHINE TRANSCARBAMYLASE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1akm/pdb
PDB entry 1akm coloured by chain, front view.
PDB entry 1akm coloured by chain, side view.
PDB entry 1akm coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure at 2.8 A resolution of anabolic ornithine transcarbamylase from Escherichia coli.
Jin L, Seaton BA, Head JF
Nat Struct Biol 4 622-5 (1997)
PMID: 9253409

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137619 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine carbamoyltransferase subunit I Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 333 amino acids
Theoretical weight: 36.82 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P04391 (Residues: 2-334; Coverage: 100%)
Gene names: JW4211, argI, b4254
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P32
Unit cell:
a: 104.6Å b: 104.6Å c: 86.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.302
Expression system: Escherichia coli

Quick links

Citations

1 review citation

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases.
Shi et al. (2015)
16 other articles

5 mentions without citation

Prediction of catalytic residues using Support Vector Machine with selected protein sequence and structural properties.
Petrova et al. (2006)
4 more