Structure analysis

CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE

X-ray diffraction
2.2Å resolution
Source organism: Pisum sativum
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 19500 Å2
Buried surface area: 4300 Å2
Dissociation area: 850 Å2
Dissociation energy (ΔGdiss): -5 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): -47 kcal/mol
Symmetry number: 2
Assembly 2
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly

Macromolecules

Chains: A, B, C, D
Length: 249 amino acids
Theoretical weight: 27.1 KDa
Source organism: Pisum sativum
Expression system: Escherichia coli
UniProt:
  • Canonical: P48534 (Residues: 2-250; Coverage: 100%)
Gene names: APPX1, APX1
Pfam: Peroxidase
InterPro:
CATH:
SCOP: CCP-like

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