Structure analysis

Crystal structure of phosphoenolpyruvate mutase complexed with Mg(II)

X-ray diffraction
2.1Å resolution
Source organism: Mytilus edulis
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo tetramer
Accessible surface area: 39800 Å2
Buried surface area: 21200 Å2
Dissociation area: 3,600 Å2
Dissociation energy (ΔGdiss): 16 kcal/mol
Dissociation entropy (TΔSdiss): 15 kcal/mol
Interface energy (ΔGint): -121 kcal/mol
Symmetry number: 4

Macromolecules

Chains: A, B, C, D
Length: 295 amino acids
Theoretical weight: 32.95 KDa
Source organism: Mytilus edulis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P56839 (Residues: 1-295; Coverage: 100%)
Pfam: Phosphoenolpyruvate phosphomutase
InterPro:
CATH: Phosphoenolpyruvate-binding domains
SCOP: Phosphoenolpyruvate mutase/Isocitrate lyase-like

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