Structure analysis

The crystal structure of engineered cytochrome c peroxidase from Saccharomyces cerevisiae with Trp51 to S-Trp51 and Trp191Phe modifications

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

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 12716.7 Å2
Buried surface area: 1947.1 Å2
Dissociation area: 107.85 Å2
Dissociation energy (ΔGdiss): -2.89 kcal/mol
Dissociation entropy (TΔSdiss): -0.01 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132475

Macromolecules

Chain: A
Length: 321 amino acids
Theoretical weight: 36.72 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P00431 (Residues: 71-361; Coverage: 81%)
Gene names: CCP, CCP1, CPO, YKR066C
Pfam: Peroxidase
InterPro:

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