› 1ad1

X-ray diffraction
2.2Å resolution

DIHYDROPTEROATE SYNTHETASE (APO FORM) FROM STAPHYLOCOCCUS AUREUS

Released:
DOI: 10.2210/pdb1ad1/pdb
Model geometry
Fit model/data
PDB entry 1ad1 coloured by chain, front view.
PDB entry 1ad1 coloured by chain, side view.
PDB entry 1ad1 coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Structure and function of the dihydropteroate synthase from Staphylococcus aureus.
Hampele IC, D'Arcy A, Dale GE, Kostrewa D, Nielsen J, Oefner C, Page MG, Schönfeld HJ, Stüber D, Then RL
J Mol Biol 268 21-30 (1997)
PMID: 9149138

Function and Biology Details

Reaction catalysed: 
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate
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-126492 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropteroate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 266 amino acids
Theoretical weight: 29.4 KDa
Source organism: Staphylococcus aureus
UniProt:
  • Canonical: O05701 (Residues: 2-267; Coverage: 100%)
Gene names: dpsA, folP
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

2 bound ligands:
Ligand K 2 x K
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: P21
Unit cell:
a: 64.47Å b: 42.19Å c: 101.32Å
α: 90° β: 106.33° γ: 90°
R-values:
R R work R free
0.159 0.159 0.218

Quick links

Citations

19 review citations

Antibiotic resistance in Staphylococcus aureus. Current status and future prospects.
Foster TJ. (2017)
18 more

5 mentions without citation

Protein subunit interfaces: heterodimers versus homodimers.
Zhanhua et al. (2005)
4 more