Magnesium in PDB 6ddc: Crystal Structure of the Single Mutant (D52N) of NT5C2-537X in the Basal State, Northeast Structural Genomics Consortium Target

All present enzymatic activity of Crystal Structure of the Single Mutant (D52N) of NT5C2-537X in the Basal State, Northeast Structural Genomics Consortium Target:
3.1.3.5;

The structure of Crystal Structure of the Single Mutant (D52N) of NT5C2-537X in the Basal State, Northeast Structural Genomics Consortium Target, PDB code: 6ddc 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, Northeast Structural Genomics Consortium (Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.42 / 2.91
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	144.555, 124.151, 90.736, 90.00, 116.25, 90.00
R / Rfree (%)	18.1 / 26.4

The binding sites of Magnesium atom in the Crystal Structure of the Single Mutant (D52N) of NT5C2-537X in the Basal State, Northeast Structural Genomics Consortium Target (pdb code 6ddc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Single Mutant (D52N) of NT5C2-537X in the Basal State, Northeast Structural Genomics Consortium Target, PDB code: 6ddc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Single Mutant (D52N) of NT5C2-537X in the Basal State, Northeast Structural Genomics Consortium Target


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 Single Mutant (D52N) of NT5C2-537X in the Basal State, Northeast Structural Genomics Consortium Target within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:34.5 occ:1.00 OD1 A:ASP351 2.4 43.7 1.0 O1 A:PO4602 2.4 36.8 1.0 O A:ASP54 2.5 34.5 1.0 CE1 A:HIS352 2.7 50.8 1.0 ND2 A:ASN52 2.7 28.2 1.0 ND1 A:HIS352 3.2 55.0 1.0 CG A:ASP351 3.3 42.9 1.0 OD2 A:ASP351 3.5 44.6 1.0 C A:ASP54 3.5 29.6 1.0 NE2 A:HIS352 3.8 49.2 1.0 P A:PO4602 3.8 42.4 1.0 O A:HOH786 3.8 68.1 1.0 CG A:ASN52 3.8 43.6 1.0 CB A:ASP54 3.9 30.0 1.0 O A:HOH778 4.0 25.3 1.0 OD1 A:ASN52 4.1 68.9 1.0 O4 A:PO4602 4.1 49.9 1.0 CA A:ASP54 4.2 29.0 1.0 CG A:HIS352 4.4 49.3 1.0 CB A:TYR55 4.5 23.8 1.0 O3 A:PO4602 4.5 32.1 1.0 N A:ASP54 4.5 31.5 1.0 N A:TYR55 4.6 22.6 1.0 CD2 A:HIS352 4.7 52.6 1.0 CB A:ASP351 4.7 37.9 1.0 O2 A:PO4602 4.8 37.6 1.0 OG1 A:THR56 4.9 23.7 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Single Mutant (D52N) of NT5C2-537X in the Basal State, Northeast Structural Genomics Consortium Target


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Single Mutant (D52N) of NT5C2-537X in the Basal State, Northeast Structural Genomics Consortium Target within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:28.6 occ:1.00 OD1 B:ASP351 2.1 37.8 1.0 ND2 B:ASN52 2.1 31.0 1.0 O B:ASP54 2.4 11.4 1.0 O1 B:PO4602 2.7 51.0 1.0 O4 B:PO4602 3.2 60.6 1.0 CG B:ASN52 3.2 39.8 1.0 CG B:ASP351 3.3 36.1 1.0 ND1 B:HIS352 3.3 55.8 1.0 CE1 B:HIS352 3.4 53.7 1.0 OD1 B:ASN52 3.5 53.4 1.0 P B:PO4602 3.5 52.3 1.0 C B:ASP54 3.6 16.9 1.0 OD2 B:ASP351 3.8 34.5 1.0 CB B:ASP54 4.2 33.3 1.0 CA B:ASP54 4.2 22.6 1.0 N B:ASP54 4.3 23.9 1.0 O2 B:PO4602 4.4 39.6 1.0 CB B:ASP351 4.5 32.5 1.0 CB B:ASN52 4.5 19.6 1.0 OG1 B:THR56 4.6 39.8 1.0 CG B:HIS352 4.6 54.2 1.0 N B:TYR55 4.6 19.9 1.0 CB B:TYR55 4.7 19.0 1.0 O3 B:PO4602 4.7 39.5 1.0 NE2 B:HIS352 4.7 56.8 1.0 N B:ASP351 4.9 11.1 1.0

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