Magnesium in PDB 1ko5: Crystal Structure of Gluconate Kinase

All present enzymatic activity of Crystal Structure of Gluconate Kinase:
2.7.1.12;

The structure of Crystal Structure of Gluconate Kinase, PDB code: 1ko5 was solved by L.Kraft, G.A.Sprenger, Y.Lindqvist, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.28
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.274, 89.206, 51.479, 90.00, 105.14, 90.00
R / Rfree (%)	21.4 / 27.7

The binding sites of Magnesium atom in the Crystal Structure of Gluconate Kinase (pdb code 1ko5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Gluconate Kinase, PDB code: 1ko5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Gluconate Kinase


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 Gluconate Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1001 b:25.1 occ:1.00 O A:HOH1018 1.9 30.1 1.0 O A:HOH1033 1.9 13.3 1.0 O1B A:ATP302 2.0 17.5 1.0 O3G A:ATP302 2.1 23.4 1.0 OG A:SER22 2.2 22.3 1.0 O A:HOH1011 2.4 15.9 1.0 PG A:ATP302 3.0 27.3 1.0 PB A:ATP302 3.1 18.8 1.0 O3B A:ATP302 3.3 23.8 1.0 CB A:SER22 3.3 19.1 1.0 O2G A:ATP302 3.5 30.6 1.0 O2A A:ATP302 3.9 24.2 1.0 N A:SER22 4.0 19.4 1.0 O3A A:ATP302 4.1 23.3 1.0 CA A:SER22 4.2 20.3 1.0 O2B A:ATP302 4.2 22.4 1.0 O1A A:ATP302 4.3 24.6 1.0 O1G A:ATP302 4.3 27.8 1.0 PA A:ATP302 4.3 24.3 1.0 O A:HOH1002 4.4 18.1 1.0 O A:HOH1041 4.4 26.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Gluconate Kinase


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 Gluconate Kinase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1002 b:28.4 occ:1.00 O B:HOH1036 1.7 28.4 1.0 O1B B:ATP303 1.9 23.7 1.0 O B:HOH1035 2.0 17.2 1.0 O3G B:ATP303 2.0 29.1 1.0 O B:HOH1025 2.2 13.0 1.0 OG B:SER22 2.3 27.1 1.0 PG B:ATP303 3.0 29.5 1.0 PB B:ATP303 3.1 24.0 1.0 CB B:SER22 3.2 26.8 1.0 O2G B:ATP303 3.4 31.9 1.0 O3B B:ATP303 3.4 28.8 1.0 N B:SER22 4.0 26.2 1.0 O2A B:ATP303 4.1 25.4 1.0 O2B B:ATP303 4.1 26.4 1.0 CA B:SER22 4.2 26.9 1.0 O3A B:ATP303 4.2 26.1 1.0 O B:HOH1012 4.2 26.7 1.0 O1G B:ATP303 4.3 27.2 1.0 PA B:ATP303 4.4 27.2 1.0 O1A B:ATP303 4.5 24.9 1.0 CG1 B:VAL86 4.8 19.2 1.0 NZ B:LYS21 4.9 17.4 1.0 CE B:LYS21 4.9 19.3 1.0 CB B:LYS21 4.9 25.1 1.0

L.Kraft, G.A.Sprenger, Y.Lindqvist. Conformational Changes During the Catalytic Cycle of Gluconate Kinase As Revealed By X-Ray Crystallography. J.Mol.Biol. V. 318 1057 2002.
ISSN: ISSN 0022-2836
PubMed: 12054802
DOI: 10.1016/S0022-2836(02)00215-2