2p10

X-ray diffraction
2.15Å resolution

CRYSTAL STRUCTURE OF A PUTATIVE PHOSPHONOPYRUVATE HYDROLASE (MLL9387) FROM MESORHIZOBIUM LOTI MAFF303099 AT 2.15 A RESOLUTION

Released:
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-189113 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
TIM-barrel domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 286 amino acids
Theoretical weight: 31.14 KDa
Source organism: Mesorhizobium japonicum MAFF 303099
Expression system: Escherichia coli
UniProt:
  • Canonical: Q981G2 (Residues: 1-285; Coverage: 100%)
Gene name: mll9387
Sequence domains: Phosphoenolpyruvate hydrolase-like
Structure domains:

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: R3
Unit cell:
a: 180.269Å b: 180.269Å c: 185.514Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.162 0.204
Expression system: Escherichia coli