› 3aez

X-ray diffraction
2.2Å resolution

Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with GDP and Phosphopantothenate

Released:
DOI: 10.2210/pdb3aez/pdb
PDB entry 3aez coloured by chain, front view.
PDB entry 3aez coloured by chain, side view.
PDB entry 3aez coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
M. tuberculosis pantothenate kinase: dual substrate specificity and unusual changes in ligand locations.
Chetnani B, Kumar P, Surolia A, Vijayan M
J Mol Biol 400 171-85 (2010)
PMID: 20451532

Function and Biology Details

Reaction catalysed: 
ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161936 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pantothenate kinase Chain: A
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 35.7 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPA7 (Residues: 1-312; Coverage: 100%)
Gene names: MTV017.45c, Rv1092c, coaA
Sequence domains: Phosphoribulokinase / Uridine kinase family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

4 bound ligands:
Ligand GDP 1 x GDP
Ligand PAZ 1 x PAZ
Ligand GOL 13 x GOL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P3121
Unit cell:
a: 103.64Å b: 103.64Å c: 90.41Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.243
Expression system: Escherichia coli

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Citations

2 review citations

Recent advances in targeting coenzyme A biosynthesis and utilization for antimicrobial drug development.
Moolman et al. (2014)
1 more

1 mention without citation

Withdrawn
(2012)