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Atomistry » Magnesium » PDB 5l5u-5lcd » 5lc8 » |
Magnesium in PDB 5lc8: Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A ResolutionEnzymatic activity of Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution
All present enzymatic activity of Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution:
1.13.11.12; 1.13.11.13; Protein crystallography data
The structure of Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution, PDB code: 5lc8
was solved by
J.Kalms,
S.Banthiya,
E.Galemou Yoga,
H.Kuhn,
P.Scheerer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5lc8:
The structure of Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution
(pdb code 5lc8). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution, PDB code: 5lc8: Magnesium binding site 1 out of 1 in 5lc8Go back to Magnesium Binding Sites List in 5lc8
Magnesium binding site 1 out
of 1 in the Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution
Mono view Stereo pair view
Reference:
J.Kalms,
S.Banthiya,
E.Galemou Yoga,
M.Hamberg,
H.G.Holzhutter,
H.Kuhn,
P.Scheerer.
The Crystal Structure of Pseudomonas Aeruginosa Lipoxygenase ALA420GLY Mutant Explains the Improved Oxygen Affinity and the Altered Reaction Specificity. Biochim. Biophys. Acta V.1862 463 2017.
Page generated: Sun Sep 29 19:49:49 2024
ISSN: ISSN 0006-3002 PubMed: 28093240 DOI: 10.1016/J.BBALIP.2017.01.003 |
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