› 1fg7

X-ray diffraction
1.5Å resolution

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

Released:
DOI: 10.2210/pdb1fg7/pdb
PDB entry 1fg7 coloured by chain, front view.
PDB entry 1fg7 coloured by chain, side view.
PDB entry 1fg7 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate.
Sivaraman J, Li Y, Larocque R, Schrag JD, Cygler M, Matte A
J Mol Biol 311 761-76 (2001)
PMID: 11518529

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: 39.58 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 PMP 1 x PMP
No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2
Unit cell:
a: 132.168Å b: 62.575Å c: 45.284Å
α: 90° β: 104.14° γ: 90°
R-values:
R R work R free
0.205 0.205 0.219
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes.
Liang et al. (2019)
18 other articles

4 mentions without citation

Contribution of structural genomics to understanding the biology of Escherichia coli.
Matte et al. (2003)
3 more