Magnesium in PDB 6wbs: Human Cftr First Nucleotide Binding Domain with DF508/V510D

All present enzymatic activity of Human Cftr First Nucleotide Binding Domain with DF508/V510D:
5.6.1.6;

The structure of Human Cftr First Nucleotide Binding Domain with DF508/V510D, PDB code: 6wbs was solved by K.S.Simon, M.Kothe, B.Hilbert, J.D.Batchelor, G.D.Hurlbut, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.77 / 1.86
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.396, 81.66, 100.404, 90, 90, 90
R / Rfree (%)	17 / 21.3

The binding sites of Magnesium atom in the Human Cftr First Nucleotide Binding Domain with DF508/V510D (pdb code 6wbs). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human Cftr First Nucleotide Binding Domain with DF508/V510D, PDB code: 6wbs:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Human Cftr First Nucleotide Binding Domain with DF508/V510D


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Cftr First Nucleotide Binding Domain with DF508/V510D within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg702 b:13.5 occ:1.00 OG1 A:THR465 2.0 16.1 1.0 NE2 A:GLN493 2.0 15.9 1.0 O2G A:ATP701 2.0 17.8 1.0 O2B A:ATP701 2.1 12.2 1.0 O A:HOH830 2.1 10.6 1.0 O A:HOH842 2.2 16.3 1.0 HE21 A:GLN493 2.4 19.0 1.0 CD A:GLN493 3.1 23.8 1.0 CB A:THR465 3.1 14.4 1.0 HB A:THR465 3.1 17.3 1.0 PG A:ATP701 3.3 19.4 1.0 PB A:ATP701 3.3 17.6 1.0 H A:THR465 3.3 15.6 1.0 OE1 A:GLN493 3.5 25.6 1.0 O3B A:ATP701 3.5 18.4 1.0 N A:THR465 3.9 13.0 1.0 HG21 A:THR465 3.9 17.8 1.0 OD2 A:ASP572 4.0 17.0 1.0 OD1 A:ASP572 4.0 14.3 1.0 O1A A:ATP701 4.0 20.2 1.0 O A:HOH905 4.1 20.6 1.0 O1G A:ATP701 4.1 18.8 1.0 CA A:THR465 4.1 13.1 1.0 HB2 A:LYS464 4.1 13.4 1.0 CG2 A:THR465 4.1 14.8 1.0 O3A A:ATP701 4.3 14.9 1.0 O A:HOH972 4.4 58.4 1.0 CG A:GLN493 4.4 23.2 1.0 O3G A:ATP701 4.4 22.0 1.0 HA A:THR465 4.4 15.7 1.0 O1B A:ATP701 4.4 14.7 1.0 HE2 A:LYS464 4.4 19.9 1.0 CG A:ASP572 4.5 17.3 1.0 HG2 A:GLN493 4.5 27.9 1.0 HB3 A:GLN493 4.6 20.6 1.0 HG23 A:THR465 4.6 17.8 1.0 O A:HOH1012 4.6 42.0 1.0 PA A:ATP701 4.6 18.6 1.0 HG11 A:VAL603 4.8 17.0 1.0 HG A:SER573 4.8 28.5 0.5 HG22 A:THR465 4.9 17.8 1.0

Magnesium binding site 2 out of 2 in the Human Cftr First Nucleotide Binding Domain with DF508/V510D


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Cftr First Nucleotide Binding Domain with DF508/V510D within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg702 b:14.6 occ:1.00 NE2 B:GLN493 1.9 15.7 1.0 O2B B:ATP701 2.0 13.5 1.0 OG1 B:THR465 2.1 14.6 1.0 O2G B:ATP701 2.1 18.1 1.0 O B:HOH870 2.1 15.9 1.0 HE21 B:GLN493 2.2 18.9 1.0 O B:HOH818 2.2 19.0 1.0 HB B:THR465 3.0 19.9 1.0 CB B:THR465 3.1 16.6 1.0 CD B:GLN493 3.1 24.1 1.0 PB B:ATP701 3.2 15.1 1.0 PG B:ATP701 3.2 21.4 1.0 H B:THR465 3.3 15.5 1.0 O3B B:ATP701 3.5 18.0 1.0 OE1 B:GLN493 3.6 27.5 1.0 N B:THR465 3.9 12.9 1.0 O1A B:ATP701 3.9 18.1 1.0 OD2 B:ASP572 4.0 22.4 1.0 HG21 B:THR465 4.0 23.8 1.0 CA B:THR465 4.1 16.1 1.0 O1G B:ATP701 4.1 25.9 1.0 O B:HOH963 4.1 37.2 1.0 CG2 B:THR465 4.2 19.9 1.0 O B:HOH847 4.2 20.5 1.0 OD1 B:ASP572 4.2 19.6 1.0 O3A B:ATP701 4.2 17.2 1.0 HB2 B:LYS464 4.2 17.4 1.0 O B:HOH983 4.3 32.5 1.0 HG2 B:GLN493 4.3 31.9 1.0 O3G B:ATP701 4.3 23.9 1.0 HA B:THR465 4.4 19.3 1.0 CG B:GLN493 4.4 26.6 1.0 O1B B:ATP701 4.4 14.9 1.0 HE2 B:LYS464 4.5 20.0 1.0 CG B:ASP572 4.5 21.4 1.0 PA B:ATP701 4.6 18.4 1.0 HG23 B:THR465 4.6 23.8 1.0 HB3 B:GLN493 4.7 32.2 1.0 O B:HOH806 4.8 50.5 1.0 HG11 B:VAL603 4.9 16.6 1.0 HG22 B:THR465 4.9 23.8 1.0 O B:HOH904 4.9 42.6 1.0

K.S.Simon, K.Nagarajan, I.Mechin, C.Duffy, P.Manavalan, S.Altmann, A.Majewski, J.Foley, J.S.Kaczmarak, S.Bercury, M.Maderia, B.Hilbert, J.D.Batchelor, R.Ziegler, J.Bajko, M.Kothe, R.Scheule, A.Nair, G.D.Hurlbut. Determining the Molecular Mechanism of Suppressor Mutation V510D and the Contribution of Helical Unraveling to the DF508-Cftr Defect To Be Published.