Magnesium in PDB 8gps: Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense

The structure of Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense, PDB code: 8gps was solved by M.Wang, Y.Zhao, M.Hattori, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.86 / 1.39
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	57.503, 57.503, 118.252, 90, 90, 120
R / Rfree (%)	18.4 / 23.2

The binding sites of Magnesium atom in the Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense (pdb code 8gps). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense, PDB code: 8gps:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:53.1 occ:1.00 O A:HOH629 2.0 35.5 1.0 O A:HOH431 2.1 29.1 1.0 O A:HOH627 2.1 32.0 1.0 O A:HOH587 2.1 28.8 1.0 O A:HOH593 2.1 43.8 1.0 O A:HOH449 2.3 28.2 1.0 O A:HOH589 2.7 68.7 1.0 O A:HOH604 3.6 42.0 1.0 O A:HOH564 3.7 36.5 1.0 OD1 A:ASP228 3.9 32.5 1.0 O A:HOH551 4.1 40.6 1.0 O A:HOH531 4.1 29.1 1.0 O A:HOH622 4.2 46.6 1.0 CB A:ALA76 4.3 30.4 1.0 O A:HOH624 4.3 51.2 1.0 OD2 A:ASP225 4.4 23.9 1.0 CG A:ASP228 4.6 29.7 1.0 OD1 A:ASP73 4.7 31.0 1.0 CB A:ASP228 4.7 26.8 1.0 O A:HOH494 4.7 30.4 1.0

Magnesium binding site 2 out of 5 in the Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:31.2 occ:1.00 O A:HIS183 2.0 31.8 1.0 O A:HOH455 2.1 34.1 1.0 O A:HOH448 2.1 27.9 1.0 OD2 A:ASP181 2.1 38.1 1.0 O A:HOH497 2.1 32.2 1.0 OD1 A:ASP160 2.2 28.1 1.0 CG A:ASP181 3.0 39.3 1.0 CG A:ASP160 3.2 30.1 1.0 OD1 A:ASP181 3.2 41.0 1.0 C A:HIS183 3.2 32.2 1.0 OD2 A:ASP160 3.4 32.9 1.0 N A:HIS183 3.9 40.9 1.0 O A:ASP161 4.0 30.9 1.0 CA A:HIS183 4.0 37.1 1.0 N A:PHE184 4.2 29.1 1.0 CA A:PHE184 4.3 26.5 1.0 O A:HOH470 4.3 41.6 1.0 O A:HOH618 4.4 71.9 1.0 N A:ASP161 4.4 25.9 1.0 CB A:HIS183 4.4 37.6 1.0 CB A:ASP181 4.4 39.2 1.0 CB A:PHE184 4.5 27.3 1.0 CB A:ASP160 4.6 29.1 1.0 O A:HOH583 4.6 30.9 1.0 N A:ASP181 4.7 40.1 1.0 N A:ASN182 4.7 44.2 1.0 C A:ASP161 4.8 28.9 1.0 CA A:ASP181 4.9 39.4 1.0 C A:ASP181 4.9 41.7 1.0 CA A:ASP160 4.9 27.7 1.0 C A:ASN182 5.0 47.1 1.0

Magnesium binding site 3 out of 5 in the Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:114.5 occ:1.00 O A:HOH462 2.0 17.9 1.0 O A:HOH446 2.0 19.6 1.0 OD1 A:ASP225 2.1 26.4 1.0 OD1 A:ASP72 2.1 24.7 1.0 O A:HOH469 2.1 20.3 1.0 O A:HOH465 2.2 19.7 1.0 CG A:ASP225 3.1 23.5 1.0 CG A:ASP72 3.2 23.9 1.0 OD2 A:ASP225 3.4 23.9 1.0 OD2 A:ASP72 3.5 27.4 1.0 MG A:MG304 3.7 70.6 1.0 O A:HOH489 3.8 18.8 1.0 OG1 A:THR222 3.8 23.4 1.0 OE1 A:GLU144 4.0 29.1 1.0 O A:HOH508 4.0 32.5 1.0 OE2 A:GLU144 4.1 27.7 1.0 OD2 A:ASP224 4.2 28.1 1.0 CD A:GLU144 4.2 27.3 1.0 OD1 A:ASP73 4.2 31.0 1.0 CB A:ASP225 4.5 20.8 1.0 CB A:ASP72 4.5 22.1 1.0 O A:HOH444 4.5 31.9 1.0 OG1 A:THR70 4.7 23.1 1.0 O A:HOH555 4.7 40.1 1.0 OD1 A:ASP224 4.8 31.5 1.0 CG A:ASP224 4.9 27.0 1.0 CG A:ASP73 4.9 27.4 1.0

Magnesium binding site 4 out of 5 in the Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:70.6 occ:1.00 O A:HOH586 2.7 53.6 1.0 O A:HOH446 2.8 19.6 1.0 O A:HOH555 2.9 40.1 1.0 O A:HOH462 3.1 17.9 1.0 O A:HOH413 3.3 83.4 1.0 OD2 A:ASP73 3.3 27.4 1.0 O A:HOH612 3.4 53.0 1.0 O A:HOH469 3.4 20.3 1.0 O A:HOH444 3.4 31.9 1.0 O A:HOH551 3.6 40.6 1.0 MG A:MG303 3.7 114.5 1.0 OD1 A:ASP73 3.9 31.0 1.0 CG A:ASP73 4.0 27.4 1.0 OD2 A:ASP224 4.2 28.1 1.0 OG1 A:THR70 4.6 23.1 1.0 OE1 A:GLU144 4.7 29.1 1.0 CG2 A:THR70 4.8 24.2 1.0 OG A:SER43 5.0 30.9 0.6 OD2 A:ASP225 5.0 23.9 1.0 O A:HOH613 5.0 32.4 1.0

Magnesium binding site 5 out of 5 in the Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Cytoplasmic Domain Structure of the Mgte MG2+ Channel From Chryseobacterium Hispalense within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg305 b:44.0 occ:1.00 O A:GLU201 2.0 25.7 1.0 O A:HOH535 2.1 23.8 1.0 OD1 A:ASP204 2.1 35.9 1.0 O A:HOH453 2.2 24.2 1.0 C A:GLU201 3.2 24.1 1.0 CG A:ASP204 3.2 28.3 1.0 OD2 A:ASP204 3.5 31.7 1.0 CA A:GLU201 3.9 26.8 1.0 CG A:GLU201 4.0 41.2 1.0 OE1 A:GLU201 4.2 49.9 1.0 O A:HOH493 4.2 25.6 1.0 N A:LYS202 4.3 22.8 1.0 CD A:GLU201 4.5 47.9 1.0 CB A:ASP204 4.5 24.7 1.0 CA A:LYS202 4.5 24.3 1.0 C A:LYS202 4.6 24.1 1.0 CB A:GLU201 4.6 31.4 1.0 O A:LYS202 4.6 26.0 1.0 O A:PHE200 4.7 24.3 1.0 N A:ASP204 4.8 25.4 1.0 CA A:ASP204 4.8 23.6 1.0

M.Wang, Y.Zhao, Y.Hayashi, K.Ito, M.Hattori. Novel MG2+ Binding Sites in the Cytoplasmic Domain of the Mgte MG2+ Channels Revealed By X-Ray Crystal Structures Acta Biochim.Biophys.Sinica 2023.
ISSN: ISSN 0582-9879
DOI: 10.3724/ABBS.2023067