› 7q2c

X-ray diffraction
1.9Å resolution

mycolic acid methyltransferase Hma (MmaA4) from Mycobac-terium tuberculosis in complex with ZT260

Released:
DOI: 10.2210/pdb7q2c/pdb
PDB entry 7q2c coloured by chain, front view.
PDB entry 7q2c coloured by chain, side view.
PDB entry 7q2c coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Fragment-Based Ligand Discovery Applied to the Mycolic Acid Methyltransferase Hma (MmaA4) from Mycobacterium tuberculosis: A Crystallographic and Molecular Modelling Study.
Galy R, Ballereau S, Génisson Y, Mourey L, Plaquevent JC, Maveyraud L
OpenAccess logo Pharmaceuticals (Basel) 14 (2021)
PMID: 34959681

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181263 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxymycolate synthase MmaA4 Chain: A
Molecule details ›
Chain: A
Length: 318 amino acids
Theoretical weight: 36.52 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q79FX8 (Residues: 4-301; Coverage: 99%)
Gene names: Rv0642c, hma, mma4, mmaA4
Sequence domains: Mycolic acid cyclopropane synthetase

Ligands and Environments

2 bound ligands:
Ligand DMS 3 x DMS
Ligand 3AV 2 x 3AV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3121
Unit cell:
a: 57.111Å b: 57.111Å c: 205.897Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.179 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.
Yan et al. (2022)

1 mention without citation

Fragment-Based Ligand Discovery Applied to the Mycolic Acid Methyltransferase Hma (MmaA4) from Mycobacterium tuberculosis: A Crystallographic and Molecular Modelling Study.
Galy et al. (2021)