› 1ep9

X-ray diffraction
2.4Å resolution

HUMAN ORNITHINE TRANSCARBAMYLASE: CRYSTALLOGRAPHIC INSIGHTS INTO SUBSTRATE RECOGNITION AND CONFORMATIONAL CHANGE

Released:
DOI: 10.2210/pdb1ep9/pdb
PDB entry 1ep9 coloured by chain, front view.
PDB entry 1ep9 coloured by chain, side view.
PDB entry 1ep9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human ornithine transcarbamylase: crystallographic insights into substrate recognition and conformational changes.
Shi D, Morizono H, Yu X, Tong L, Allewell NM, Tuchman M
Biochem J 354 501-9 (2001)
PMID: 11237854

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 CP 1 x CP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P213
Unit cell:
a: 125.6Å b: 125.6Å c: 125.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.223
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Mechanistic insights into the regulation of metabolic enzymes by acetylation.
Xiong et al. (2012)
5 more

10 mentions without citation

Zinc-binding cysteines: diverse functions and structural motifs.
Pace et al. (2014)
9 more