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: 19508.51 Å2
Buried surface area: 4250.97 Å2
Dissociation area: 865.35 Å2
Dissociation energy (ΔGdiss): -6.13 kcal/mol
Dissociation entropy (TΔSdiss): 12.94 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-155749
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 19777.67 Å2
Buried surface area: 4197.9 Å2
Dissociation area: 836.8 Å2
Dissociation energy (ΔGdiss): -5.55 kcal/mol
Dissociation entropy (TΔSdiss): 12.93 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-155749

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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