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Magnesium in PDB 1ko8: Crystal Structure of Gluconate Kinase

Enzymatic activity of Crystal Structure of Gluconate Kinase

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

Protein crystallography data

The structure of Crystal Structure of Gluconate Kinase, PDB code: 1ko8 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) 25.00 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.790, 89.120, 51.560, 90.00, 109.69, 90.00
R / Rfree (%) 25.4 / 30.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Gluconate Kinase (pdb code 1ko8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Gluconate Kinase, PDB code: 1ko8:

Magnesium binding site 1 out of 1 in 1ko8

Go back to Magnesium Binding Sites List in 1ko8
Magnesium binding site 1 out of 1 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:Mg201

b:58.8
occ:1.00
O A:HOH516 1.7 42.0 1.0
O A:HOH512 2.0 40.2 1.0
O3P A:6PG502 2.0 44.4 1.0
OG A:SER22 2.2 44.9 1.0
O A:HOH513 2.4 45.5 1.0
O A:HOH515 3.0 38.4 1.0
O A:HOH514 3.1 45.1 1.0
CB A:SER22 3.2 44.1 1.0
P A:6PG502 3.2 43.0 1.0
O2P A:6PG502 3.6 42.1 1.0
O6 A:6PG502 3.6 44.8 1.0
O A:HOH517 3.7 39.6 1.0
N A:SER22 4.0 44.3 1.0
OD2 A:ASP38 4.2 49.7 1.0
CA A:SER22 4.3 44.1 1.0
OD2 A:ASP40 4.3 50.8 1.0
O1P A:6PG502 4.4 39.8 1.0
OD1 A:ASP38 4.5 48.8 1.0
C6 A:6PG502 4.8 47.1 1.0
CG A:ASP38 4.9 46.5 1.0

Reference:

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
Page generated: Sun Aug 10 00:25:40 2025

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