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Atomistry » Potassium » PDB 6bd3-6csr » 6ci0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 6bd3-6csr » 6ci0 » |
Potassium in PDB 6ci0: Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with E101A (II) MutationEnzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with E101A (II) Mutation
All present enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with E101A (II) Mutation:
1.9.3.1; Protein crystallography data
The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with E101A (II) Mutation, PDB code: 6ci0
was solved by
J.Liu,
C.Hiser,
S.Ferguson-Miller,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6ci0:
The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with E101A (II) Mutation also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with E101A (II) Mutation
(pdb code 6ci0). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with E101A (II) Mutation, PDB code: 6ci0: Potassium binding site 1 out of 1 in 6ci0Go back to Potassium Binding Sites List in 6ci0
Potassium binding site 1 out
of 1 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with E101A (II) Mutation
Mono view Stereo pair view
Reference:
C.Hiser,
J.Liu,
S.Ferguson-Miller.
The K-Path Entrance in Cytochrome C Oxidase Is Defined By Mutation of E101 and Controlled By An Adjacent Ligand Binding Domain. Biochim. Biophys. Acta V.1859 725 2018.
Page generated: Mon Aug 12 15:34:34 2024
ISSN: ISSN 0006-3002 PubMed: 29626419 DOI: 10.1016/J.BBABIO.2018.03.017 |
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