Magnesium in PDB 4gkr: Structure of the C-Terminal Motor Domain of KAR3 From Candida Glabrata

The structure of Structure of the C-Terminal Motor Domain of KAR3 From Candida Glabrata, PDB code: 4gkr was solved by D.Duan, J.S.Allingham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.69
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.707, 84.066, 151.127, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 25.7

The binding sites of Magnesium atom in the Structure of the C-Terminal Motor Domain of KAR3 From Candida Glabrata (pdb code 4gkr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the C-Terminal Motor Domain of KAR3 From Candida Glabrata, PDB code: 4gkr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of the C-Terminal Motor Domain of KAR3 From Candida Glabrata


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the C-Terminal Motor Domain of KAR3 From Candida Glabrata within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg701 b:33.6 occ:1.00 O A:HOH808 1.8 25.9 1.0 O A:HOH816 2.0 23.5 1.0 O A:HOH823 2.0 28.8 1.0 O A:HOH815 2.1 15.2 1.0 O2B A:ADP702 2.1 28.1 1.0 OG1 A:THR442 2.3 34.0 1.0 PB A:ADP702 3.3 29.0 1.0 CB A:THR442 3.5 33.2 1.0 O3B A:ADP702 3.5 27.2 1.0 O A:HOH809 3.7 30.7 1.0 O A:HOH801 4.0 26.7 1.0 N A:THR442 4.1 30.8 1.0 O2A A:ADP702 4.3 30.2 1.0 CA A:THR442 4.3 31.4 1.0 O3A A:ADP702 4.3 30.7 1.0 O1B A:ADP702 4.3 30.0 1.0 OD2 A:ASP589 4.4 52.1 1.0 OD1 A:ASP589 4.5 54.2 1.0 CG2 A:THR442 4.5 33.5 1.0 PA A:ADP702 4.6 31.1 1.0 O A:HOH821 4.7 49.7 1.0 O A:HOH822 4.8 39.3 1.0 CE A:LYS441 4.8 29.2 1.0 NZ A:LYS441 4.9 30.6 1.0 CG A:ASP589 4.9 47.3 1.0 CA A:SER560 4.9 34.1 1.0 O1A A:ADP702 4.9 32.4 1.0 CB A:LYS441 4.9 28.7 1.0

Magnesium binding site 2 out of 2 in the Structure of the C-Terminal Motor Domain of KAR3 From Candida Glabrata


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the C-Terminal Motor Domain of KAR3 From Candida Glabrata within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg701 b:26.3 occ:1.00 O B:HOH812 1.8 26.2 1.0 O B:HOH804 2.1 25.3 1.0 O B:HOH823 2.1 21.9 1.0 OG1 B:THR442 2.1 26.6 1.0 O B:HOH813 2.3 20.5 1.0 O2B B:ADP702 2.3 23.7 1.0 O3B B:ADP702 2.9 22.1 1.0 PB B:ADP702 3.1 22.7 1.0 CB B:THR442 3.3 28.6 1.0 O2A B:ADP702 3.9 26.2 1.0 N B:THR442 4.0 26.4 1.0 O B:HOH822 4.2 40.3 1.0 O3A B:ADP702 4.2 25.8 1.0 O B:ARG548 4.2 41.7 1.0 CA B:THR442 4.3 28.0 1.0 O1B B:ADP702 4.3 24.2 1.0 CG2 B:THR442 4.4 28.1 1.0 O B:HOH805 4.4 22.1 1.0 PA B:ADP702 4.5 27.1 1.0 OD2 B:ASP589 4.5 48.2 1.0 OD1 B:ASP589 4.7 47.2 1.0 O1A B:ADP702 4.8 27.1 1.0 NZ B:LYS441 4.8 22.2 1.0 CB B:LYS441 4.9 23.8 1.0 CE B:LYS441 4.9 21.9 1.0

D.Duan, Z.Jia, M.Joshi, J.Brunton, M.Chan, D.Drew, D.Davis, J.S.Allingham. Neck Rotation and Neck Mimic Docking in the Noncatalytic KAR3-Associated Protein VIK1. J.Biol.Chem. V. 287 40292 2012.
ISSN: ISSN 0021-9258
PubMed: 23043140
DOI: 10.1074/JBC.M112.416529