› 5ett

X-ray diffraction
1.55Å resolution

S. aureus 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.55 angstrom resolution

Released:
DOI: 10.2210/pdb5ett/pdb
PDB entry 5ett coloured by chain, front view.
PDB entry 5ett coloured by chain, side view.
PDB entry 5ett coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Structural Basis for the Selective Binding of Inhibitors to 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase from Staphylococcus aureus and Escherichia coli.
Dennis ML, Pitcher NP, Lee MD, DeBono AJ, Wang ZC, Harjani JR, Rahmani R, Cleary B, Peat TS, Baell JB, Swarbrick JD
J Med Chem 59 5248-63 (2016)
PMID: 27094768

Function and Biology Details

Reaction catalysed: 
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173505 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 161 amino acids
Theoretical weight: 18.3 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2G0Q5 (Residues: 1-158; Coverage: 100%)
Gene name: SAOUHSC_00491
Sequence domains: 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK)
Structure domains: 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK

Ligands and Environments

4 bound ligands:
Ligand APC 2 x APC
Ligand 5RY 2 x 5RY
Ligand NA 3 x NA
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 47.546Å b: 68.404Å c: 53.125Å
α: 90° β: 105.94° γ: 90°
R-values:
R R work R free
0.16 0.158 0.192
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

The Structural and Functional Basis for Recurring Sulfa Drug Resistance Mutations in Staphylococcus aureus Dihydropteroate Synthase.
Griffith et al. (2018)
7 more