› 1ac8

X-ray diffraction
2.1Å resolution

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

Released:
DOI: 10.2210/pdb1ac8/pdb
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
Primary publication:
Variation in strength of an unconventional C-H to O hydrogen bond in an engineered protein cavity
Fitzgerald MM, Musah RA, McRee DE, Goodin DB
J. Am. Chem. Soc. 119 626-631 (1997)

Function and Biology Details

Reaction catalysed: 
2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132475 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c peroxidase, mitochondrial Chain: A
Molecule details ›
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
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand TMZ 1 x TMZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 108Å b: 77.3Å c: 51.8Å
α: 90° β: 90° γ: 90°
Expression system: Escherichia coli BL21(DE3)

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Citations

3 mentions without citation

Probing molecular docking in a charged model binding site.
Brenk et al. (2006)
2 more