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VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (3,4,5-TRIMETHYLTHIAZOLE)

X-ray diffraction
2.1Å resolution
PDB entry 1ac8 coloured by chain, front view.
PDB entry 1ac8 coloured by chain, side view.
PDB entry 1ac8 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: 12340.49 Å2
Buried surface area: 1667.26 Å2
Dissociation area: 212.39 Å2
Dissociation energy (ΔGdiss): -4.34 kcal/mol
Dissociation entropy (TΔSdiss): 1.6 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132475

Macromolecules

Cytochrome c peroxidase, mitochondrial
Chain: A
Length: 294 amino acids
Theoretical weight: 33.46 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
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 1ac8, assembly 1, front view.
Cytochrome c peroxidase, mitochondrial in PDB entry 1ac8, assembly 1, side view.
Cytochrome c peroxidase, mitochondrial in PDB entry 1ac8, assembly 1, top view.
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