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4hb7

X-ray diffraction
1.95Å resolution

The Structure of Dihydropteroate Synthase from Staphylococcus aureus subsp. aureus Mu50.

Released:
Model geometry
Fit model/data
Entry authors: Cuff ME, Holowicki J, Jedrzejczak R, Terwilliger TC, Rubin EJ, Guinn K, Baker D, Ioerger TR, Sacchettini JC, Joachimiak A, Midwest Center for Structural Genomics (MCSG), Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors (MTBI)

Function and Biology Details

Reaction catalysed:
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-159127 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropteroate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 270 amino acids
Theoretical weight: 29.84 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P64141 (Residues: 1-267; Coverage: 100%)
Gene names: SAV0514, folP
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 90.584Å b: 77.301Å c: 90.546Å
α: 90° β: 99.75° γ: 90°
R-values:
R R work R free
0.164 0.162 0.206
Expression system: Escherichia coli BL21(DE3)