Magnesium in PDB 6de3: Crystal Structure of the Double Mutant (R39Q/D52N) of the Full-Length NT5C2 in the Active State

Enzymatic activity of Crystal Structure of the Double Mutant (R39Q/D52N) of the Full-Length NT5C2 in the Active State

All present enzymatic activity of Crystal Structure of the Double Mutant (R39Q/D52N) 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 (R39Q/D52N) of the Full-Length NT5C2 in the Active State, PDB code: 6de3 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:

Resolution Low / High (Å) 46.18 / 3.06
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 92.362, 129.098, 131.016, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 22.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Double Mutant (R39Q/D52N) of the Full-Length NT5C2 in the Active State (pdb code 6de3). 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 (R39Q/D52N) of the Full-Length NT5C2 in the Active State, PDB code: 6de3:

Magnesium binding site 1 out of 1 in 6de3

Go back to Magnesium Binding Sites List in 6de3
Magnesium binding site 1 out of 1 in the Crystal Structure of the Double Mutant (R39Q/D52N) of the Full-Length NT5C2 in the Active State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Double Mutant (R39Q/D52N) of the Full-Length NT5C2 in the Active State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:40.3
occ:0.50
O1B A:ATP602 2.1 50.2 1.0
O1G A:ATP602 2.3 51.2 1.0
O3B A:ATP602 3.0 56.7 1.0
PB A:ATP602 3.1 52.6 1.0
PG A:ATP602 3.2 46.3 1.0
O2G A:ATP602 3.7 37.8 1.0
O3A A:ATP602 4.1 57.4 1.0
OH A:TYR457 4.1 51.7 1.0
O2B A:ATP602 4.2 57.9 1.0
NH2 A:ARG456 4.4 55.9 1.0
NZ A:LYS362 4.4 58.7 1.0
O3G A:ATP602 4.5 27.9 1.0

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.
ISSN: ISSN 1878-3686
PubMed: 29990496
DOI: 10.1016/J.CCELL.2018.06.003
Page generated: Mon Dec 14 22:34:44 2020

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