Chlorine in PDB 3tyk: Crystal Structure of Aminoglycoside Phosphotransferase Aph(4)-Ia

All present enzymatic activity of Crystal Structure of Aminoglycoside Phosphotransferase Aph(4)-Ia:
2.7.1.163;

The structure of Crystal Structure of Aminoglycoside Phosphotransferase Aph(4)-Ia, PDB code: 3tyk was solved by P.J.Stogios, I.G.Shabalin, T.Shakya, E.Evdokmova, Y.Fan, M.Chruszcz, W.Minor, G.D.Wright, A.Savchenko, W.F.Anderson, Midwest Center Forstructural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.01 / 1.95
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	70.640, 70.640, 125.880, 90.00, 90.00, 120.00
R / Rfree (%)	15.7 / 20.3

The binding sites of Chlorine atom in the Crystal Structure of Aminoglycoside Phosphotransferase Aph(4)-Ia (pdb code 3tyk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Aminoglycoside Phosphotransferase Aph(4)-Ia, PDB code: 3tyk:

Chlorine binding site 1 out of 1 in the Crystal Structure of Aminoglycoside Phosphotransferase Aph(4)-Ia


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 Aminoglycoside Phosphotransferase Aph(4)-Ia within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl343 b:39.6 occ:1.00 O A:HOH574 2.9 54.4 1.0 N A:GLN139 3.2 32.0 1.0 C A:GLY137 3.3 34.5 1.0 N A:ILE141 3.3 26.1 1.0 CA A:GLY137 3.4 34.1 1.0 N A:GLY137 3.5 30.7 1.0 N A:PRO138 3.6 32.7 1.0 N A:GLY140 3.6 27.2 1.0 O A:GLY137 3.6 32.4 1.0 CB A:GLN139 3.6 39.8 1.0 CA A:GLN139 3.7 35.0 1.0 O A:ILE141 3.7 27.2 1.0 CB A:ILE141 3.7 28.1 1.0 CD A:PRO138 3.8 37.8 1.0 C A:GLN139 3.8 31.6 1.0 O A:HOH522 3.8 47.8 1.0 CA A:ILE141 3.9 25.9 1.0 CG1 A:ILE141 4.1 29.6 1.0 C A:ILE141 4.2 25.4 1.0 C A:PRO138 4.3 31.6 1.0 CG A:GLN139 4.3 48.4 1.0 C A:GLY140 4.4 26.5 1.0 CA A:PRO138 4.5 31.7 1.0 O A:GLN139 4.5 32.7 1.0 CA A:GLY140 4.5 26.8 1.0 CD1 A:ILE141 4.7 30.5 1.0 CG A:PRO138 4.7 38.2 1.0 C A:PHE136 4.8 27.1 1.0

P.J.Stogios, T.Shakya, E.Evdokimova, A.Savchenko, G.D.Wright. Structure and Function of Aph(4)-Ia, A Hygromycin B Resistance Enzyme. J.Biol.Chem. V. 286 1966 2011.
ISSN: ISSN 0021-9258
PubMed: 21084294