› 1gew

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE

Released:
DOI: 10.2210/pdb1gew/pdb
PDB entry 1gew coloured by chain, front view.
PDB entry 1gew coloured by chain, side view.
PDB entry 1gew coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme.
Haruyama K, Nakai T, Miyahara I, Hirotsu K, Mizuguchi H, Hayashi H, Kagamiyama H
Biochemistry 40 4633-44 (2001)
PMID: 11294630

Function and Biology Details

Reaction catalysed: 
L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
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-139323 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphate aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 356 amino acids
Theoretical weight: 39.39 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06986 (Residues: 1-356; Coverage: 100%)
Gene names: JW2003, b2021, hisC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 133.33Å b: 63.82Å c: 46.2Å
α: 90° β: 104.07° γ: 90°
R-values:
R R work R free
0.202 0.197 0.247
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

3 mentions without citation

Structural Consideration of the Working Mechanism of Fold Type I Transaminases From Eubacteria: Overt and Covert Movement.
Kwon et al. (2019)
2 more