› 1oth

X-ray diffraction
1.85Å resolution

CRYSTAL STRUCTURE OF HUMAN ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ORNITHINE

Released:
DOI: 10.2210/pdb1oth/pdb
PDB entry 1oth coloured by chain, front view.
PDB entry 1oth coloured by chain, side view.
PDB entry 1oth coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
1.85-A resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-ornithine. Catalytic mechanism and correlation with inherited deficiency.
Shi D, Morizono H, Ha Y, Aoyagi M, Tuchman M, Allewell NM
J Biol Chem 273 34247-54 (1998)
PMID: 9852088

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-132546 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine transcarbamylase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 36.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00480 (Residues: 34-354; Coverage: 91%)
Gene name: OTC
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

1 bound ligand:
Ligand PAO 1 x PAO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P213
Unit cell:
a: 125.9Å b: 125.9Å c: 125.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.201
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Almost all about citrulline in mammals.
Curis et al. (2005)
5 more

22 mentions without citation

Ornithine Transcarbamylase - From Structure to Metabolism: An Update.
Couchet et al. (2021)
21 more