3otw

X-ray diffraction
1.8Å resolution

Structural and Functional Studies of Helicobacter pylori Wild-Type and Mutated Proteins Phosphopantetheine adenylyltransferase

Released:
Source organism: Helicobacter pylori 26695
Entry authors: Yin HS, Cheng CS, Chen CG, Luo YC, Chen WT, Cheng SY

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-127811 (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: 163 amino acids
Theoretical weight: 18.52 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli
UniProt:
  • Canonical: O26010 (Residues: 1-157; Coverage: 100%)
Gene names: HP_1475, coaD, kdtB
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 77.419Å b: 119.846Å c: 124.573Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.186 0.222
Expression system: Escherichia coli