› 1h1c

X-ray diffraction
2.85Å resolution

Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima

Released:
DOI: 10.2210/pdb1h1c/pdb
PDB entry 1h1c coloured by chain, front view.
PDB entry 1h1c coloured by chain, side view.
PDB entry 1h1c coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase.
Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M
J Biol Chem 279 21478-88 (2004)
PMID: 15007066

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194697 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphate aminotransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 335 amino acids
Theoretical weight: 39.77 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0D0 (Residues: 1-335; Coverage: 100%)
Gene names: TM_1040, hisC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
No bound ligands
1 modified residue:
Ligand MSE 36 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P21212
Unit cell:
a: 189.666Å b: 146.168Å c: 54.292Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.258 0.258 0.272
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
1 more

1 mention without citation

Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities.
Nasir et al. (2016)