› 1q7g

X-ray diffraction
2.6Å resolution

Homoserine Dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-Oxonorvaline

Released:
DOI: 10.2210/pdb1q7g/pdb
PDB entry 1q7g coloured by chain, front view.
PDB entry 1q7g coloured by chain, side view.
PDB entry 1q7g coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Enzyme-assisted suicide: molecular basis for the antifungal activity of 5-hydroxy-4-oxonorvaline by potent inhibition of homoserine dehydrogenase.
Jacques SL, Mirza IA, Ejim L, Koteva K, Hughes DW, Green K, Kinach R, Honek JF, Lai HK, Berghuis AM, Wright GD
Chem Biol 10 989-95 (2003)
PMID: 14583265

Function and Biology Details

Reaction catalysed: 
L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H
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-151909 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homoserine dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 359 amino acids
Theoretical weight: 38.54 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P31116 (Residues: 1-359; Coverage: 100%)
Gene names: HOM6, J2132, YJR139C
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NA 2 x NA
Ligand NHO 1 x NHO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P43212
Unit cell:
a: 80.863Å b: 80.863Å c: 248.986Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.247 0.306
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Drug targets in mycobacterial sulfur metabolism.
Bhave et al. (2007)
5 more

2 mentions without citation

Exploring the molecular basis for selective binding of homoserine dehydrogenase from Mycobacterium leprae TN toward inhibitors: a virtual screening study.
Zhan et al. (2014)
1 more