› 1c9y

X-ray diffraction
1.9Å resolution

HUMAN ORNITHINE TRANSCARBAMYLASE: CRYSTALLOGRAPHIC INSIGHTS INTO SUBSTRATE RECOGNITION AND CATALYTIC MECHANISM

Released:
DOI: 10.2210/pdb1c9y/pdb
PDB entry 1c9y coloured by chain, front view.
PDB entry 1c9y coloured by chain, side view.
PDB entry 1c9y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human ornithine transcarbamylase complexed with carbamoyl phosphate and L-norvaline at 1.9 A resolution.
Shi D, Morizono H, Aoyagi M, Tuchman M, Allewell NM
Proteins 39 271-7 (2000)
PMID: 10813810

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

2 bound ligands:
Ligand NVA 1 x NVA
Ligand CP 1 x CP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P213
Unit cell:
a: 125.41Å b: 125.41Å c: 125.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.208
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Ornithine and its role in metabolic diseases: An appraisal.
Sivashanmugam et al. (2017)
2 more

11 mentions without citation

Intricate knots in proteins: Function and evolution.
Virnau et al. (2006)
10 more