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Atomistry » Magnesium » PDB 1nzz-1oev » 1ocj » |
Magnesium in PDB 1ocj: Mutant D416A of the Cellobiohydrolase CEL6A From Humicola Insolens in Complex with A Thiopentasaccharide at 1.3 Angstrom ResolutionEnzymatic activity of Mutant D416A of the Cellobiohydrolase CEL6A From Humicola Insolens in Complex with A Thiopentasaccharide at 1.3 Angstrom Resolution
All present enzymatic activity of Mutant D416A of the Cellobiohydrolase CEL6A From Humicola Insolens in Complex with A Thiopentasaccharide at 1.3 Angstrom Resolution:
3.2.1.91; Protein crystallography data
The structure of Mutant D416A of the Cellobiohydrolase CEL6A From Humicola Insolens in Complex with A Thiopentasaccharide at 1.3 Angstrom Resolution, PDB code: 1ocj
was solved by
A.Varrot,
T.P.Frandsen,
I.Von Ossowski,
V.Boyer,
H.Driguez,
M.Schulein,
G.J.Davies,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Mutant D416A of the Cellobiohydrolase CEL6A From Humicola Insolens in Complex with A Thiopentasaccharide at 1.3 Angstrom Resolution
(pdb code 1ocj). 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 Mutant D416A of the Cellobiohydrolase CEL6A From Humicola Insolens in Complex with A Thiopentasaccharide at 1.3 Angstrom Resolution, PDB code: 1ocj: Magnesium binding site 1 out of 1 in 1ocjGo back to Magnesium Binding Sites List in 1ocj
Magnesium binding site 1 out
of 1 in the Mutant D416A of the Cellobiohydrolase CEL6A From Humicola Insolens in Complex with A Thiopentasaccharide at 1.3 Angstrom Resolution
Mono view Stereo pair view
Reference:
A.Varrot,
T.P.Frandsen,
I.Von Ossowski,
V.Boyer,
H.Driguez,
M.Schulein,
G.J.Davies.
Structural Basis For Ligand Binding and Processivity in Cellobiohydrolase CEL6A From Humicola Insolens Structure V. 11 855 2003.
Page generated: Tue Aug 13 10:36:24 2024
ISSN: ISSN 0969-2126 PubMed: 12842048 DOI: 10.1016/S0969-2126(03)00124-2 |
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