› 1k23

X-ray diffraction
3Å resolution

Inorganic Pyrophosphatase (Family II) from Bacillus subtilis

Released:
DOI: 10.2210/pdb1k23/pdb
PDB entry 1k23 coloured by chain, front view.
PDB entry 1k23 coloured by chain, side view.
PDB entry 1k23 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
The "open" and "closed" structures of the type-C inorganic pyrophosphatases from Bacillus subtilis and Streptococcus gordonii.
Ahn S, Milner AJ, Fütterer K, Konopka M, Ilias M, Young TW, White SA
J Mol Biol 313 797-811 (2001)
PMID: 11697905

Function and Biology Details

Reaction catalysed: 
Diphosphate + H(2)O = 2 phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153417 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Manganese-dependent inorganic pyrophosphatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 309 amino acids
Theoretical weight: 34.26 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P37487 (Residues: 1-309; Coverage: 100%)
Gene names: BSU40550, ppaC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MN 8 x MN
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 80.29Å b: 130.56Å c: 150.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.26 0.26 0.293
Expression system: Escherichia coli

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Citations

3 review citations

Inorganic pyrophosphatases: one substrate, three mechanisms.
Kajander et al. (2013)
2 more

12 mentions without citation

"Protein" no longer means what it used to.
Parisi et al. (2021)
11 more