› 3coz

X-ray diffraction
2Å resolution

Crystal Structure of Mycobacterium Tuberculosis Pantothenate Synthetase at 2.0 Ang resolution- in complex with sulphonamide inhibitor 4

Released:
DOI: 10.2210/pdb3coz/pdb
PDB entry 3coz coloured by chain, front view.
PDB entry 3coz coloured by chain, side view.
PDB entry 3coz coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Inhibition of Mycobacterium tuberculosis pantothenate synthetase by analogues of the reaction intermediate.
Ciulli A, Scott DE, Ando M, Reyes F, Saldanha SA, Tuck KL, Chirgadze DY, Blundell TL, Abell C
Chembiochem 9 2606-11 (2008)
PMID: 18821554

Function and Biology Details

Reaction catalysed: 
ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161641 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pantothenate synthetase Chains: A, B
Molecule details ›
Chains: A, B
Length: 301 amino acids
Theoretical weight: 31.57 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WIL5 (Residues: 1-300; Coverage: 97%)
Gene names: MTCY07H7B.20, Rv3602c, panC
Sequence domains: Pantoate-beta-alanine ligase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SO4 2 x SO4
Ligand 54H 2 x 54H
Ligand GOL 1 x GOL
Ligand EOH 4 x EOH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 48.6Å b: 71.23Å c: 82.02Å
α: 90° β: 99.56° γ: 90°
R-values:
R R work R free
0.17 0.168 0.218
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Structural biology in fragment-based drug design.
Murray et al. (2010)
11 more

4 mentions without citation

Inhibition of Mycobacterium tuberculosis pantothenate synthetase by analogues of the reaction intermediate.
Ciulli et al. (2008)
3 more