› 1h73

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH THREONINE

Released:
DOI: 10.2210/pdb1h73/pdb
PDB entry 1h73 coloured by chain, front view.
PDB entry 1h73 coloured by chain, side view.
PDB entry 1h73 coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
Structural basis for the catalysis and substrate specificity of homoserine kinase.
Krishna SS, Zhou T, Daugherty M, Osterman A, Zhang H
Biochemistry 40 10810-8 (2001)
PMID: 11535056

Function and Biology Details

Reaction catalysed: 
ATP + L-homoserine = ADP + O-phospho-L-homoserine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homoserine kinase Chain: A
Molecule details ›
Chain: A
Length: 296 amino acids
Theoretical weight: 32.3 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q58504 (Residues: 1-296; Coverage: 100%)
Gene names: MJ1104, thrB
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand THR 1 x THR
Ligand ANP 1 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 88.642Å b: 88.642Å c: 99.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.222
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Structure and function of enzymes of the Leloir pathway for galactose metabolism.
Holden et al. (2003)
4 more

1 mention without citation

Reduction of Feedback Inhibition in Homoserine Kinase (ThrB) of Corynebacterium glutamicum Enhances l-Threonine Biosynthesis.
Petit et al. (2018)