Magnesium in PDB 2q0h: Abc Protein Artp in Complex with Adp/MG2+, Atp-Gamma-S Hydrolyzed

All present enzymatic activity of Abc Protein Artp in Complex with Adp/MG2+, Atp-Gamma-S Hydrolyzed:
3.6.3.21;

The structure of Abc Protein Artp in Complex with Adp/MG2+, Atp-Gamma-S Hydrolyzed, PDB code: 2q0h was solved by P.F.Thaben, V.Eckey, F.Scheffel, W.Saenger, E.Schneider, A.Vahedi-Faridi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.428, 84.007, 69.535, 90.00, 105.60, 90.00
R / Rfree (%)	23.3 / 27.5

The binding sites of Magnesium atom in the Abc Protein Artp in Complex with Adp/MG2+, Atp-Gamma-S Hydrolyzed (pdb code 2q0h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Abc Protein Artp in Complex with Adp/MG2+, Atp-Gamma-S Hydrolyzed, PDB code: 2q0h:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Abc Protein Artp in Complex with Adp/MG2+, Atp-Gamma-S Hydrolyzed


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Abc Protein Artp in Complex with Adp/MG2+, Atp-Gamma-S Hydrolyzed within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:43.9 occ:1.00 O2B A:ADP401 2.3 32.2 1.0 O A:HOH520 2.4 34.9 1.0 OG A:SER41 2.4 28.4 1.0 O A:HOH553 2.4 26.2 1.0 O A:HOH503 2.6 28.6 1.0 O2A A:ADP401 3.1 38.1 1.0 CB A:SER41 3.1 27.7 1.0 O1B A:ADP401 3.2 36.4 1.0 PB A:ADP401 3.3 32.6 1.0 OD1 B:ASP135 3.8 45.8 0.5 O3A A:ADP401 4.2 39.1 1.0 PA A:ADP401 4.2 34.9 1.0 CG B:ASP135 4.3 46.6 0.5 N A:SER41 4.3 25.6 1.0 OD2 B:ASP135 4.3 48.9 0.5 CA A:SER41 4.3 25.8 1.0 O A:HOH534 4.4 50.8 1.0 O3B A:ADP401 4.5 38.7 1.0 OE2 A:GLU162 4.6 31.7 1.0 OD2 A:ASP161 4.6 22.7 1.0 O A:HOH680 4.8 54.5 1.0 OD1 A:ASP161 4.8 24.4 1.0 O A:HOH685 4.8 49.0 1.0 O1A A:ADP401 4.8 37.7 1.0 NH1 A:ARG45 4.9 39.2 1.0 O A:HOH590 5.0 53.4 1.0

Magnesium binding site 2 out of 2 in the Abc Protein Artp in Complex with Adp/MG2+, Atp-Gamma-S Hydrolyzed


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Abc Protein Artp in Complex with Adp/MG2+, Atp-Gamma-S Hydrolyzed within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg404 b:38.7 occ:1.00 O B:HOH577 2.2 31.4 1.0 OG B:SER41 2.3 35.5 1.0 O B:HOH535 2.4 37.5 1.0 O A:HOH552 2.4 33.5 1.0 O B:HOH534 2.4 35.5 1.0 O3B B:ADP402 2.5 41.1 1.0 PB B:ADP402 3.2 37.5 1.0 O1B B:ADP402 3.2 41.6 1.0 CB B:SER41 3.2 34.8 1.0 O2A B:ADP402 3.5 48.4 1.0 OE2 B:GLU162 4.1 36.3 1.0 N B:SER41 4.1 35.4 1.0 O B:HOH579 4.2 41.8 1.0 CA B:SER41 4.2 35.8 1.0 OD1 B:ASP161 4.3 27.4 1.0 O3A B:ADP402 4.3 41.7 1.0 O B:HOH506 4.4 25.1 1.0 OD2 B:ASP161 4.4 28.9 1.0 O2B B:ADP402 4.4 40.6 1.0 O B:HOH519 4.5 35.3 1.0 OD1 A:ASP135 4.5 59.5 1.0 PA B:ADP402 4.5 47.0 1.0 O A:HOH560 4.6 43.4 1.0 OD2 A:ASP135 4.7 60.5 1.0 CG A:ASP135 4.7 57.7 1.0 CG B:ASP161 4.8 28.9 1.0 O B:HOH525 4.8 41.2 1.0

P.F.Thaben, V.Eckey, F.Scheffel, W.Saenger, E.Schneider, A.Vahedi-Faridi. Crystal Structures of the Atp-Binding Cassette (Abc) Protein Artp From Geobacillus Stearothermophilus Reveal A Stable Dimer in the Post Hydrolysis State and An Asymmetry in the Dimerization Region To Be Published.