› 1pym

X-ray diffraction
1.8Å resolution

PHOSPHOENOLPYRUVATE MUTASE FROM MOLLUSK IN WITH BOUND MG2-OXALATE

Released:
DOI: 10.2210/pdb1pym/pdb
PDB entry 1pym coloured by chain, front view.
PDB entry 1pym coloured by chain, side view.
PDB entry 1pym coloured by chain, top view.
Source organism: Mytilus edulis
Primary publication:
Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate.
Huang K, Li Z, Jia Y, Dunaway-Mariano D, Herzberg O
Structure 7 539-48 (1999)
PMID: 10378273

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate = 3-phosphonopyruvate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate phosphomutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 33.28 KDa
Source organism: Mytilus edulis
Expression system: Escherichia coli
UniProt:
  • Canonical: P56839 (Residues: 1-295; Coverage: 100%)
Sequence domains: Phosphoenolpyruvate phosphomutase
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

2 bound ligands:
Ligand OXL 2 x OXL
Ligand MG 2 x MG
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2221
Unit cell:
a: 90.4Å b: 131.1Å c: 90.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.256
Expression system: Escherichia coli

Quick links

Citations

2 review citations

3D domain swapping: as domains continue to swap.
Liu et al. (2002)
1 more

2 mentions without citation

3D domain swapping in the TIM barrel of the α subunit of Streptococcus pneumoniae tryptophan synthase.
Michalska et al. (2020)
1 more