› 3nd6

X-ray diffraction
2.3Å resolution

Crystal structure of phosphopantetheine adenylyltransferase (PPAT) in complex with ATP from Enterococcus faecalis

Released:
DOI: 10.2210/pdb3nd6/pdb
PDB entry 3nd6 coloured by chain, front view.
PDB entry 3nd6 coloured by chain, side view.
PDB entry 3nd6 coloured by chain, top view.
Source organism: Enterococcus faecalis
Primary publication:
Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine.
Yoon HJ, Kang JY, Mikami B, Lee HH, Suh SW
Mol Cells 32 431-5 (2011)
PMID: 21912874

Function and Biology Details

Reaction catalysed: 
ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182773 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphopantetheine adenylyltransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 171 amino acids
Theoretical weight: 19.77 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q831P9 (Residues: 1-163; Coverage: 100%)
Gene names: EF_2451, coaD
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

1 bound ligand:
Ligand ATP 6 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 112.793Å b: 123.906Å c: 124.233Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.245
Expression system: Escherichia coli

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Citations

1 review citation

Structural Biology and the Design of New Therapeutics: From HIV and Cancer to Mycobacterial Infections: A Paper Dedicated to John Kendrew.
Thomas et al. (2017)
3 other articles

2 mentions without citation

Discovery of inhibitors of 4'-phosphopantetheine adenylyltransferase (PPAT) to validate PPAT as a target for antibacterial therapy.
de Jonge et al. (2013)
1 more