› 5w8o

X-ray diffraction
1.47Å resolution

Homoserine transacetylase MetX from Mycobacterium hassiacum

Released:
DOI: 10.2210/pdb5w8o/pdb
PDB entry 5w8o coloured by chain, front view.
PDB entry 5w8o coloured by chain, side view.
PDB entry 5w8o coloured by chain, top view.
Source organism: Mycolicibacterium hassiacum DSM 44199
Primary publication:
Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site.
Chaton CT, Rodriguez ES, Reed RW, Li J, Kenner CW, Korotkov KV
Sci Rep 9 20267 (2019)
PMID: 31889085

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homoserine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 363 amino acids
Theoretical weight: 38.34 KDa
Source organism: Mycolicibacterium hassiacum DSM 44199
Expression system: Escherichia coli
UniProt:
  • Canonical: K5B926 (Residues: 13-372; Coverage: 96%)
Gene names: C731_1248, MHAS_00417, metX, metXA, metX_2
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand NA 2 x NA
Ligand CA 4 x CA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 47.75Å b: 93.23Å c: 81.59Å
α: 90° β: 94.78° γ: 90°
R-values:
R R work R free
0.154 0.153 0.183
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Molecular targets for antifungals in amino acid and protein biosynthetic pathways.
Kuplińska et al. (2021)
1 more

2 mentions without citation

Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site.
Chaton et al. (2019)
1 more