› 5etn

X-ray diffraction
1.4Å resolution

E. coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.40 angstrom resolution

Released:
DOI: 10.2210/pdb5etn/pdb
PDB entry 5etn coloured by chain, front view.
PDB entry 5etn coloured by chain, side view.
PDB entry 5etn coloured by chain, top view.
Source organism: Escherichia coli
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-150686 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 18.31 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P26281 (Residues: 1-159; Coverage: 100%)
Gene names: JW0138, b0142, folK
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 CA 4 x CA
Ligand ATP 1 x ATP
Ligand 5RX 1 x 5RX
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 35.88Å b: 57.89Å c: 38.61Å
α: 90° β: 115.12° γ: 90°
R-values:
R R work R free
0.184 0.182 0.219
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