› 6ki8

X-ray diffraction
1.79Å resolution

Pyrophosphatase mutant K149R from Acinetobacter baumannii

Released:
DOI: 10.2210/pdb6ki8/pdb
PDB entry 6ki8 coloured by chain, front view.
PDB entry 6ki8 coloured by chain, side view.
PDB entry 6ki8 coloured by chain, top view.
Source organism: Acinetobacter baumannii
Primary publication:
Crystal Structures of Pyrophosphatase from Acinetobacter baumannii: Snapshots of Pyrophosphate Binding and Identification of a Phosphorylated Enzyme Intermediate.
Si Y, Wang X, Yang G, Yang T, Li Y, Ayala GJ, Li X, Wang H, Su J
Int J Mol Sci 20 (2019)
PMID: 31500178

Function and Biology Details

Reaction catalysed: 
Diphosphate + H(2)O = 2 phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100847 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inorganic pyrophosphatase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 177 amino acids
Theoretical weight: 19.53 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0A7XPH7 (Residues: 1-174; Coverage: 99%)
Gene names: AE32_00191, AL533_16370, IG607_12960, SAMEA104305365_03515, ppa
Sequence domains: Inorganic pyrophosphatase

Ligands and Environments

2 bound ligands:
Ligand DPO 3 x DPO
Ligand MG 9 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P41212
Unit cell:
a: 116.755Å b: 116.755Å c: 109.704Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.158 0.182
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Characterization of a family I inorganic pyrophosphatase from Legionella pneumophila Philadelphia 1.
Moorefield et al. (2023)

1 mention without citation

Crystal Structures of Pyrophosphatase from Acinetobacter baumannii: Snapshots of Pyrophosphate Binding and Identification of a Phosphorylated Enzyme Intermediate.
Si et al. (2019)