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Structure paper

TitleThe K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1859, Page 725-733, Year 2018
Publish dateFeb 23, 2018 (structure data deposition date)
AuthorsHiser, C. / Liu, J. / Ferguson-Miller, S.
External linksBiochim. Biophys. Acta / PubMed:29626419
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-6ci0:
Catalytic core subunits (I and II) of cytochrome C oxidase from Rhodobacter sphaeroides with E101A (II) mutation
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-DMU:
DECYL-BETA-D-MALTOPYRANOSIDE / detergent*YM

ChemComp-TRD:
TRIDECANE

ChemComp-CU:
COPPER (II) ION

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-HEA:
HEME-A

ChemComp-CD:
Unknown entry

ChemComp-HTH:
(2S,3R)-heptane-1,2,3-triol

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

Source
  • rhodobacter sphaeroides (bacteria)
KeywordsOXIDOREDUCTASE / Oxidase / electron transfer / proton pumping

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