› 5vve

X-ray diffraction
1.7Å resolution

Crystal structure of phosphoglycerate mutase from Naegleria fowleri

Released:
DOI: 10.2210/pdb5vve/pdb
PDB entry 5vve coloured by chain, front view.
PDB entry 5vve coloured by chain, side view.
PDB entry 5vve coloured by chain, top view.
Source organism: Naegleria fowleri
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed: 
(1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-N(tau)-phospho-L-histidine + 2/3-phospho-D-glycerate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104174 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate mutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 258 amino acids
Theoretical weight: 30 KDa
Source organism: Naegleria fowleri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A2D0TCG6 (Residues: 1-250; Coverage: 100%)
Gene names: FDP41_009301, NF0048460
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand CL 1 x CL
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: I222
Unit cell:
a: 77.61Å b: 89.33Å c: 157.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.195
Expression system: Escherichia coli BL21(DE3)

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