› 2can

X-ray diffraction
2.3Å resolution

HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH L-CANALINE

Released:
DOI: 10.2210/pdb2can/pdb
PDB entry 2can coloured by chain, front view.
PDB entry 2can coloured by chain, side view.
PDB entry 2can coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition.
Shah SA, Shen BW, Brünger AT
Structure 5 1067-75 (1997)
PMID: 9309222

Function and Biology Details

Reaction catalysed: 
L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137491 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine aminotransferase, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 402 amino acids
Theoretical weight: 44.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04181 (Residues: 38-439; Coverage: 92%)
Gene name: OAT
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 3 x PLP
1 bound ligand:
Ligand CAN 3 x CAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P3221
Unit cell:
a: 115.915Å b: 115.915Å c: 185.729Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.212 0.238
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Eliot et al. (2004)
7 more

6 mentions without citation

HEB in the spotlight: Transcriptional regulation of T-cell specification, commitment, and developmental plasticity.
Braunstein et al. (2012)
5 more