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Atomistry » Potassium » PDB 4l4d-4mkk » 4l4d | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 4l4d-4mkk » 4l4d » |
Potassium in PDB 4l4d: Structure of Cyanide and Camphor Bound P450CAM Mutant L358AEnzymatic activity of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A
All present enzymatic activity of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A:
1.14.15.1; Protein crystallography data
The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A, PDB code: 4l4d
was solved by
D.Batabyal,
H.Li,
T.L.Poulos,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4l4d:
The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A
(pdb code 4l4d). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A, PDB code: 4l4d: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 4l4dGo back to Potassium Binding Sites List in 4l4d
Potassium binding site 1 out
of 2 in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 4l4dGo back to Potassium Binding Sites List in 4l4d
Potassium binding site 2 out
of 2 in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A
Mono view Stereo pair view
Reference:
D.Batabyal,
H.Li,
T.L.Poulos.
Synergistic Effects of Mutations in Cytochrome P450CAM Designed to Mimic CYP101D1. Biochemistry V. 52 5396 2013.
Page generated: Sun Dec 13 23:39:59 2020
ISSN: ISSN 0006-2960 PubMed: 23865948 DOI: 10.1021/BI400676D |
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