Magnesium in PDB 6ds1: Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+

The structure of Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+, PDB code: 6ds1 was solved by B.Pluvinage, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.46 / 2.12
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	68.504, 68.462, 70.718, 89.31, 113.43, 115.67
R / Rfree (%)	15.9 / 21.4

The binding sites of Magnesium atom in the Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+ (pdb code 6ds1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+, PDB code: 6ds1:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:20.1 occ:1.00 N A:ASP62 3.3 28.1 1.0 ND2 A:ASN65 3.4 25.5 1.0 CG1 A:ILE61 3.5 28.2 1.0 O A:ASP62 3.7 27.4 1.0 CA A:ILE61 3.9 22.8 1.0 CG A:GLN68 4.1 22.1 1.0 CB A:ASN65 4.1 23.0 1.0 C A:ILE61 4.1 24.4 1.0 CA A:ASP62 4.2 30.9 1.0 CG A:ASN65 4.2 29.5 1.0 CB A:ASP62 4.3 27.7 1.0 CB A:ILE61 4.3 24.6 1.0 C A:ASP62 4.3 24.5 1.0 CD1 A:ILE61 4.6 38.2 1.0 CB A:GLN68 4.8 21.9 1.0 O A:HOH482 4.8 31.3 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:23.1 occ:1.00 ND2 B:ASN65 3.2 23.0 1.0 N B:ASP62 3.3 24.1 1.0 CG1 B:ILE61 3.6 29.7 1.0 O B:ASP62 3.7 26.9 1.0 CA B:ILE61 3.8 23.7 1.0 C B:ILE61 4.1 25.9 1.0 CB B:ASN65 4.1 22.6 1.0 CA B:ASP62 4.2 26.1 1.0 CG B:ASN65 4.2 26.0 1.0 CB B:ILE61 4.2 23.1 1.0 CB B:ASP62 4.3 28.2 1.0 CG B:GLN68 4.3 25.1 1.0 C B:ASP62 4.3 25.4 1.0 CD1 B:ILE61 4.7 42.1 1.0 CB B:GLN68 5.0 25.5 1.0 O B:GLU60 5.0 25.5 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+ within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg302 b:20.5 occ:1.00 CD1 C:ILE61 3.0 46.2 1.0 N C:ASP62 3.3 27.4 1.0 ND2 C:ASN65 3.4 27.0 1.0 O C:ASP62 3.9 28.8 1.0 CA C:ILE61 4.0 25.3 1.0 CB C:ASP62 4.1 27.7 1.0 CA C:ASP62 4.1 30.4 1.0 CB C:ASN65 4.2 22.2 1.0 C C:ILE61 4.2 25.5 1.0 CG C:GLN68 4.2 24.4 1.0 CG1 C:ILE61 4.2 33.3 1.0 CG C:ASN65 4.3 29.1 1.0 C C:ASP62 4.4 26.7 1.0 CB C:ILE61 4.6 30.5 1.0 O C:HOH513 4.7 41.5 1.0 CB C:GLN68 4.9 21.7 1.0 O C:HOH487 4.9 34.2 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of CJ0485 Dehydrogenase in Complex with Nadp+ within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg304 b:20.7 occ:1.00 N D:ASP62 3.2 28.8 1.0 ND2 D:ASN65 3.3 28.4 1.0 CG1 D:ILE61 3.7 30.6 1.0 O D:ASP62 3.7 23.8 1.0 CA D:ILE61 3.9 25.7 1.0 C D:ILE61 4.1 27.2 1.0 CA D:ASP62 4.1 26.1 1.0 CB D:ASN65 4.1 22.5 1.0 CB D:ASP62 4.1 27.2 1.0 CG D:GLN68 4.1 23.5 1.0 CG D:ASN65 4.2 28.0 1.0 C D:ASP62 4.3 30.4 1.0 CB D:ILE61 4.3 28.3 1.0 CD1 D:ILE61 4.8 42.1 1.0 CB D:GLN68 4.8 21.5 1.0 CD D:GLN68 5.0 25.1 1.0

J.M.Garber, H.Nothaft, B.Pluvinage, H.Huang, M.Stahl, X.Bian, J.Glushka, E.Line, A.Stintzi, J.A.Gerlt, A.B.Boraston, C.M.Szymanski. No Longer Asaccharolytic - L-Fucose and D-Arabinose Metabolism in Campylobacter Jejuni To Be Published.