Chlorine in PDB 1ko4: 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: 1ko4 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)	79.06 / 2.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	70.231, 72.602, 79.079, 90.00, 90.00, 90.00
R / Rfree (%)	24 / 30.4

The binding sites of Chlorine atom in the Crystal Structure of Gluconate Kinase (pdb code 1ko4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Gluconate Kinase, PDB code: 1ko4:
Jump to Chlorine binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Gluconate Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl176 b:17.1 occ:1.00 N A:GLY18 3.1 20.7 1.0 N A:SER19 3.3 21.1 1.0 NZ A:LYS21 3.4 11.7 1.0 N A:LYS21 3.4 18.2 1.0 N A:GLY20 3.4 20.6 1.0 O A:VAL16 3.6 19.9 1.0 CB A:LYS21 3.7 17.1 1.0 CG A:LYS21 3.8 16.0 1.0 CA A:GLY18 3.9 20.7 1.0 C A:SER17 3.9 21.2 1.0 CA A:SER17 3.9 21.4 1.0 C A:GLY18 4.0 21.1 1.0 OG A:SER19 4.0 22.4 1.0 C A:SER19 4.1 20.9 1.0 CA A:GLY20 4.1 19.8 1.0 CA A:LYS21 4.2 17.7 1.0 CA A:SER19 4.2 21.3 1.0 C A:GLY20 4.2 19.7 1.0 O A:HOH198 4.4 7.6 1.0 C A:VAL16 4.5 19.3 1.0 CE A:LYS21 4.6 14.8 1.0 N A:SER17 4.6 20.4 1.0 CB A:SER19 4.7 20.9 1.0 CD A:LYS21 4.8 14.1 1.0 N A:SER22 4.8 17.0 1.0 O A:SER17 5.0 20.7 1.0

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


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Gluconate Kinase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl176 b:25.9 occ:1.00 NZ B:LYS21 2.9 17.4 1.0 N B:GLY18 3.1 21.5 1.0 O B:HOH217 3.3 33.4 1.0 N B:GLY20 3.4 20.5 1.0 N B:LYS21 3.5 18.9 1.0 NH2 B:ARG124 3.6 54.4 1.0 N B:SER19 3.6 21.3 1.0 CA B:SER17 3.9 22.2 1.0 O B:HOH187 3.9 13.8 1.0 CE B:LYS21 3.9 14.7 1.0 C B:SER17 3.9 22.2 1.0 CB B:LYS21 3.9 19.3 1.0 OG B:SER19 4.0 21.9 1.0 CA B:GLY18 4.0 21.1 1.0 O B:VAL16 4.1 19.9 1.0 CA B:GLY20 4.1 19.2 1.0 C B:GLY20 4.1 19.4 1.0 C B:GLY18 4.2 21.3 1.0 CG B:LYS21 4.2 17.2 1.0 C B:SER19 4.3 20.8 1.0 CA B:LYS21 4.3 19.3 1.0 CA B:SER19 4.4 20.9 1.0 CD B:LYS21 4.7 15.3 1.0 N B:SER17 4.7 20.6 1.0 O B:HOH193 4.8 26.1 1.0 C B:VAL16 4.8 20.1 1.0 CZ B:ARG124 4.8 54.8 1.0 CB B:SER19 4.8 21.5 1.0 OG B:SER17 4.8 26.4 1.0 N B:SER22 4.9 21.4 1.0 CB B:SER17 4.9 22.9 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