› 1yvw

X-ray diffraction
2.6Å resolution

Crystal structure of Phosphoribosyl-ATP pyrophosphohydrolase from Bacillus cereus. NESGC target BcR13.

Released:
DOI: 10.2210/pdb1yvw/pdb
PDB entry 1yvw coloured by chain, front view.
PDB entry 1yvw coloured by chain, side view.
PDB entry 1yvw coloured by chain, top view.
Source organism: Bacillus cereus
Entry authors: Benach J, Kuzin AP, Forouhar F, Abashidze M, Vorobiev SM, Shastry R, Rong X, Acton TB, Montelione GT, Hunt JF, Northeast Structural Genomics Consortium (NESG)

Function and Biology Details

Reaction catalysed: 
1-(5-phospho-beta-D-ribosyl)-ATP + H(2)O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182521 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosyl-ATP pyrophosphatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 115 amino acids
Theoretical weight: 13.68 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q81G00 (Residues: 1-107; Coverage: 100%)
Gene names: BC_1412, hisE
Sequence domains: Phosphoribosyl-ATP pyrophosphohydrolase
Structure domains: MazG-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P6522
Unit cell:
a: 81.959Å b: 81.959Å c: 222.978Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.244 0.263
Expression system: Escherichia coli

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