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Atomistry » Magnesium » PDB 6d9m-6dlu » 6de2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 6d9m-6dlu » 6de2 » |
Magnesium in PDB 6de2: Crystal Structure of the Double Mutant (D52N/L375F) of the Full-Length NT5C2 in the Active StateEnzymatic activity of Crystal Structure of the Double Mutant (D52N/L375F) of the Full-Length NT5C2 in the Active State
All present enzymatic activity of Crystal Structure of the Double Mutant (D52N/L375F) of the Full-Length NT5C2 in the Active State:
3.1.3.5; Protein crystallography data
The structure of Crystal Structure of the Double Mutant (D52N/L375F) of the Full-Length NT5C2 in the Active State, PDB code: 6de2
was solved by
F.Forouhar,
C.L.Dieck,
G.Tzoneva,
Z.Carpenter,
A.Ambesi-Impiombato,
M.Sanchez-Martin,
R.Kirschner-Schwabe,
S.Lew,
J.Seetharaman,
A.A.Ferrando,
L.Tong,
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 Crystal Structure of the Double Mutant (D52N/L375F) of the Full-Length NT5C2 in the Active State
(pdb code 6de2). 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 the Double Mutant (D52N/L375F) of the Full-Length NT5C2 in the Active State, PDB code: 6de2: Magnesium binding site 1 out of 1 in 6de2Go back to Magnesium Binding Sites List in 6de2
Magnesium binding site 1 out
of 1 in the Crystal Structure of the Double Mutant (D52N/L375F) of the Full-Length NT5C2 in the Active State
Mono view Stereo pair view
Reference:
C.L.Dieck,
G.Tzoneva,
F.Forouhar,
Z.Carpenter,
A.Ambesi-Impiombato,
M.Sanchez-Martin,
R.Kirschner-Schwabe,
S.Lew,
J.Seetharaman,
L.Tong,
A.A.Ferrando.
Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. Cancer Cell V. 34 136 2018.
Page generated: Mon Sep 30 23:07:12 2024
ISSN: ISSN 1878-3686 PubMed: 29990496 DOI: 10.1016/J.CCELL.2018.06.003 |
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