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EFFECT OF UNNATURAL HEME SUBSTITUTION ON KINETICS OF ELECTRON TRANSFER IN CYTOCHROME C PEROXIDASE

X-ray diffraction
2.2Å resolution
PDB entry 1bek coloured by chain, front view.
PDB entry 1bek coloured by chain, side view.
PDB entry 1bek coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Cytochrome c peroxidase, mitochondrial
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Multimeric state: monomeric
Accessible surface area: 11822.78 Å2
Buried surface area: 1260.65 Å2
Dissociation area: 630.32 Å2
Dissociation energy (ΔGdiss): 19.08 kcal/mol
Dissociation entropy (TΔSdiss): 5.84 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132475

Macromolecules

Cytochrome c peroxidase, mitochondrial
Chain: A
Length: 291 amino acids
Theoretical weight: 33.13 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P00431 (Residues: 71-361; Coverage: 81%)
Gene names: CCP, CCP1, CPO, YKR066C
Pfam: Peroxidase
InterPro:
CATH:
SCOP: CCP-like
Cytochrome c peroxidase, mitochondrial in PDB entry 1bek, assembly 1, front view.
Cytochrome c peroxidase, mitochondrial in PDB entry 1bek, assembly 1, side view.
Cytochrome c peroxidase, mitochondrial in PDB entry 1bek, assembly 1, top view.
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