› 2zos

X-ray diffraction
1.7Å resolution

Crystal structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb2zos/pdb
PDB entry 2zos coloured by chain, front view.
PDB entry 2zos coloured by chain, side view.
PDB entry 2zos coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
Structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii.
Kawamura T, Watanabe N, Tanaka I
Acta Crystallogr D Biol Crystallogr 64 1267-76 (2008)
PMID: 19018103

Function and Biology Details

Reaction catalysed: 
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H(2)O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129752 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannosyl-3-phosphoglycerate phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 249 amino acids
Theoretical weight: 29.13 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O58690 (Residues: 1-243; Coverage: 100%)
Gene names: PH0926, mngB
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 58.487Å b: 68.607Å c: 67.567Å
α: 90° β: 96.48° γ: 90°
R-values:
R R work R free
0.213 0.213 0.234
Expression system: Escherichia coli

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Citations

3 review citations

Diversity, biological roles and biosynthetic pathways for sugar-glycerate containing compatible solutes in bacteria and archaea.
Empadinhas et al. (2011)
2 more