Structure analysis

Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog

X-ray diffraction
1.7Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 12400 Å2
Buried surface area: 800 Å2
Dissociation area: 250 Å2
Dissociation energy (ΔGdiss): -5 kcal/mol
Dissociation entropy (TΔSdiss): 3 kcal/mol
Interface energy (ΔGint): -12 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 261 amino acids
Theoretical weight: 28.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UHY7 (Residues: 1-261; Coverage: 100%)
Gene names: ENOPH1, MASA, MSTP145
InterPro:
CATH:
SCOP: Enolase-phosphatase E1

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