› 1x74

X-ray diffraction
1.79Å resolution

Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis- mutational and structural characterization of the fold and active site

Released:
DOI: 10.2210/pdb1x74/pdb
PDB entry 1x74 coloured by chain, front view.
PDB entry 1x74 coloured by chain, side view.
PDB entry 1x74 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis. Mutational and structural characterization of the active site and the fold.
Savolainen K, Bhaumik P, Schmitz W, Kotti TJ, Conzelmann E, Wierenga RK, Hiltunen JK
J Biol Chem 280 12611-20 (2005)
PMID: 15632186

Function and Biology Details

Reaction catalysed: 
(2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA
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-126518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-methylacyl-CoA racemase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 360 amino acids
Theoretical weight: 38.72 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: O06543 (Residues: 1-360; Coverage: 100%)
Gene names: Rv1143, mcr
Sequence domains: CoA-transferase family III
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 15 x GOL
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 180.073Å b: 79.779Å c: 117.619Å
α: 90° β: 92.04° γ: 90°
R-values:
R R work R free
0.162 0.16 0.193
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Peroxisomal beta-oxidation--a metabolic pathway with multiple functions.
Poirier et al. (2006)
3 more

2 mentions without citation

Formyl-coenzyme A (CoA):oxalate CoA-transferase from the acidophile Acetobacter aceti has a distinctive electrostatic surface and inherent acid stability.
Mullins et al. (2012)
1 more