Magnesium in PDB 2pzf: Minimal Human Cftr First Nucleotide Binding Domain As A Head-to-Tail Dimer with Delta F508

All present enzymatic activity of Minimal Human Cftr First Nucleotide Binding Domain As A Head-to-Tail Dimer with Delta F508:
3.6.3.49;

The structure of Minimal Human Cftr First Nucleotide Binding Domain As A Head-to-Tail Dimer with Delta F508, PDB code: 2pzf was solved by S.Atwell, K.Conners, S.Emtage, T.Gheyi, N.R.Glenn, J.Hendle, H.A.Lewis, F.Lu, L.A.Rodgers, R.Romero, J.M.Sauder, D.Smith, H.Tien, S.R.Wasserman, X.Zhao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.12 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.152, 92.662, 106.471, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 25.1

The binding sites of Magnesium atom in the Minimal Human Cftr First Nucleotide Binding Domain As A Head-to-Tail Dimer with Delta F508 (pdb code 2pzf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Minimal Human Cftr First Nucleotide Binding Domain As A Head-to-Tail Dimer with Delta F508, PDB code: 2pzf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Minimal Human Cftr First Nucleotide Binding Domain As A Head-to-Tail Dimer with Delta F508


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Minimal Human Cftr First Nucleotide Binding Domain As A Head-to-Tail Dimer with Delta F508 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg3 b:15.5 occ:1.00 O2G A:ATP1 2.0 17.0 1.0 O A:HOH647 2.0 16.5 1.0 O2B A:ATP1 2.0 16.9 1.0 O A:HOH648 2.1 14.5 1.0 OG1 A:THR465 2.2 14.9 1.0 OE1 A:GLN493 2.2 19.6 1.0 CD A:GLN493 3.1 16.3 1.0 PG A:ATP1 3.2 16.4 1.0 PB A:ATP1 3.2 16.5 1.0 CB A:THR465 3.3 16.9 1.0 NE2 A:GLN493 3.3 17.5 1.0 O3B A:ATP1 3.4 16.3 1.0 O1G A:ATP1 3.9 16.9 1.0 O1A A:ATP1 3.9 18.8 1.0 OD1 A:ASP572 4.0 16.2 1.0 O A:HOH649 4.0 18.4 1.0 N A:THR465 4.0 17.3 1.0 O A:HOH666 4.1 23.6 1.0 N B:GLY550 4.1 22.4 1.0 OD2 A:ASP572 4.1 17.2 1.0 O3A A:ATP1 4.2 15.8 1.0 CA A:THR465 4.3 16.4 1.0 CG2 A:THR465 4.4 19.9 1.0 O3G A:ATP1 4.4 20.3 1.0 CG A:GLN493 4.4 18.9 1.0 O1B A:ATP1 4.4 16.0 1.0 CG A:ASP572 4.4 20.1 1.0 PA A:ATP1 4.6 17.8 1.0 CA B:GLY550 4.8 21.4 1.0 CB B:SER549 4.9 22.7 1.0 CA B:SER549 5.0 23.0 1.0

Magnesium binding site 2 out of 2 in the Minimal Human Cftr First Nucleotide Binding Domain As A Head-to-Tail Dimer with Delta F508


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Minimal Human Cftr First Nucleotide Binding Domain As A Head-to-Tail Dimer with Delta F508 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg4 b:18.2 occ:1.00 O2B B:ATP2 2.0 17.6 1.0 O2G B:ATP2 2.1 19.6 1.0 O B:HOH648 2.1 15.3 1.0 OG1 B:THR465 2.1 16.7 1.0 O B:HOH647 2.2 14.0 1.0 OE1 B:GLN493 2.2 21.3 1.0 CD B:GLN493 3.1 25.4 1.0 CB B:THR465 3.2 17.0 1.0 PG B:ATP2 3.2 17.8 1.0 PB B:ATP2 3.3 19.0 1.0 NE2 B:GLN493 3.5 20.2 1.0 O3B B:ATP2 3.6 17.1 1.0 O1A B:ATP2 3.9 20.0 1.0 O1G B:ATP2 3.9 17.8 1.0 OD2 B:ASP572 4.0 16.4 1.0 N B:THR465 4.0 17.1 1.0 OD1 B:ASP572 4.0 21.5 1.0 O B:HOH649 4.1 17.8 1.0 O A:HOH680 4.1 40.0 1.0 CA B:THR465 4.1 16.3 1.0 N A:GLY550 4.2 21.4 1.0 CG2 B:THR465 4.3 17.7 1.0 CG B:GLN493 4.3 21.6 1.0 O3A B:ATP2 4.3 21.1 1.0 CG B:ASP572 4.4 18.5 1.0 O1B B:ATP2 4.4 18.1 1.0 O3G B:ATP2 4.5 20.4 1.0 PA B:ATP2 4.5 18.9 1.0 CA A:GLY550 4.9 21.0 1.0

S.Atwell, C.G.Brouillette, K.Conners, S.Emtage, T.Gheyi, W.B.Guggino, J.Hendle, J.F.Hunt, H.A.Lewis, F.Lu, I.I.Protasevich, L.A.Rodgers, R.Romero, S.R.Wasserman, P.C.Weber, D.Wetmore, F.F.Zhang, X.Zhao. Structures of A Minimal Human Cftr First Nucleotide-Binding Domain As A Monomer, Head-to-Tail Homodimer, and Pathogenic Mutant. Protein Eng.Des.Sel. V. 23 375 2010.
ISSN: ISSN 1741-0126
PubMed: 20150177
DOI: 10.1093/PROTEIN/GZQ004