3g1p

X-ray diffraction
1.4Å resolution

Crystals structure of PhnP from E.coli K-12

Released:
Source organism: Escherichia coli K-12
Entry authors: Podzelinska K, Jia Z

Function and Biology Details

Reaction catalysed:
5-phospho-alpha-D-ribose 1,2-cyclic phosphate + H(2)O = alpha-D-ribose 1,5-bisphosphate
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-147800 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 258 amino acids
Theoretical weight: 28.71 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P16692 (Residues: 1-252; Coverage: 100%)
Gene names: JW4053, b4092, phnP
Sequence domains: Beta-lactamase superfamily domain
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 111.65Å b: 75.405Å c: 83.228Å
α: 90° β: 126.33° γ: 90°
R-values:
R R work R free
0.187 0.186 0.21
Expression system: Escherichia coli