› 1i74

X-ray diffraction
2.2Å resolution

STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE

Released:
DOI: 10.2210/pdb1i74/pdb
PDB entry 1i74 coloured by chain, front view.
PDB entry 1i74 coloured by chain, side view.
PDB entry 1i74 coloured by chain, top view.
Source organism: Streptococcus mutans
Primary publication:
Crystal structure of Streptococcus mutans pyrophosphatase: a new fold for an old mechanism.
Merckel MC, Fabrichniy IP, Salminen A, Kalkkinen N, Baykov AA, Lahti R, Goldman A
Structure 9 289-97 (2001)
PMID: 11525166

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-130621 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable manganese-dependent inorganic pyrophosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 33.54 KDa
Source organism: Streptococcus mutans
Expression system: Escherichia coli
UniProt:
  • Canonical: O68579 (Residues: 2-310; Coverage: 100%)
Gene names: SMU_1687, dlt5, ppaC, ppx1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MN 4 x MN
Ligand MG 2 x MG
Ligand SO4 4 x SO4
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P212121
Unit cell:
a: 75.6Å b: 95.3Å c: 95.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.257
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

5 mentions without citation

Amino acid empirical contact energy definitions for fold recognition in the space of contact maps.
Berrera et al. (2003)
4 more