› 5etk

X-ray diffraction
1.09Å resolution

E. coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.09 angstrom resolution

Released:
DOI: 10.2210/pdb5etk/pdb
Model geometry
Fit model/data
PDB entry 5etk coloured by chain, front view.
PDB entry 5etk coloured by chain, side view.
PDB entry 5etk 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

5 bound ligands:
Ligand APC 1 x APC
Ligand 5RU 1 x 5RU
Ligand CA 4 x CA
Ligand CL 2 x CL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 35.79Å b: 57.69Å c: 38.45Å
α: 90° β: 115.57° γ: 90°
R-values:
R R work R free
0.117 0.116 0.136
Expression system: Escherichia coli

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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