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Atomistry » Strontium » PDB 8cvd-8oyr » 8cvd » |
Strontium in PDB 8cvd: Structure of Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, Succinate, and ScopolamineEnzymatic activity of Structure of Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, Succinate, and Scopolamine
All present enzymatic activity of Structure of Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, Succinate, and Scopolamine:
1.14.11.11; Protein crystallography data
The structure of Structure of Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, Succinate, and Scopolamine, PDB code: 8cvd
was solved by
E.W.Wenger,
A.K.Boal,
J.M.Bollinger,
C.Krebs,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 8cvd:
The structure of Structure of Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, Succinate, and Scopolamine also contains other interesting chemical elements:
Strontium Binding Sites:
The binding sites of Strontium atom in the Structure of Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, Succinate, and Scopolamine
(pdb code 8cvd). This binding sites where shown within
5.0 Angstroms radius around Strontium atom.
In total 2 binding sites of Strontium where determined in the Structure of Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, Succinate, and Scopolamine, PDB code: 8cvd: Jump to Strontium binding site number: 1; 2; Strontium binding site 1 out of 2 in 8cvdGo back to Strontium Binding Sites List in 8cvd
Strontium binding site 1 out
of 2 in the Structure of Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, Succinate, and Scopolamine
Mono view Stereo pair view
Strontium binding site 2 out of 2 in 8cvdGo back to Strontium Binding Sites List in 8cvd
Strontium binding site 2 out
of 2 in the Structure of Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, Succinate, and Scopolamine
Mono view Stereo pair view
Reference:
E.S.Wenger,
A.K.Boal,
J.M.Bollinger,
C.Krebs.
Structure of the H6H Cyclization Product Complex To Be Published.
Page generated: Fri Oct 11 07:47:14 2024
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