Chlorine in PDB 3m64: Human Aldose Reductase Mutant T113V Complexed with IDD393

All present enzymatic activity of Human Aldose Reductase Mutant T113V Complexed with IDD393:
1.1.1.21;

The structure of Human Aldose Reductase Mutant T113V Complexed with IDD393, PDB code: 3m64 was solved by C.Koch, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.370, 66.360, 47.200, 90.00, 92.59, 90.00
R / Rfree (%)	12.6 / 17.4

The binding sites of Chlorine atom in the Human Aldose Reductase Mutant T113V Complexed with IDD393 (pdb code 3m64). 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 Human Aldose Reductase Mutant T113V Complexed with IDD393, PDB code: 3m64:

Chlorine binding site 1 out of 1 in the Human Aldose Reductase Mutant T113V Complexed with IDD393


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Aldose Reductase Mutant T113V Complexed with IDD393 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl600 b:8.4 occ:1.00 CL1 A:393600 0.0 8.4 1.0 C13 A:393600 1.7 7.3 1.0 C15 A:393600 2.7 7.8 1.0 C12 A:393600 2.7 7.2 1.0 O A:VAL47 3.1 6.2 1.0 O A:HOH1020 3.5 10.6 1.0 O A:HOH1010 3.5 9.9 1.0 NE1 A:TRP20 3.7 6.8 1.0 C A:VAL47 3.8 4.7 1.0 CD1 A:TYR48 3.8 6.5 1.0 CD1 A:TRP20 3.8 5.7 1.0 CA A:TYR48 3.9 4.1 1.0 CG1 A:VAL47 3.9 5.8 1.0 C16 A:393600 4.0 7.4 1.0 C11 A:393600 4.0 8.1 1.0 N A:TYR48 4.1 5.0 1.0 CG2 A:VAL47 4.2 7.2 1.0 O A:HOH1008 4.4 9.7 1.0 CE1 A:TYR48 4.5 5.3 1.0 C10 A:393600 4.5 8.0 1.0 CB A:VAL47 4.5 6.3 1.0 O A:HOH1122 4.7 14.5 1.0 CA A:VAL47 4.7 5.3 1.0 CG A:TYR48 4.7 4.8 1.0 CE2 A:TRP20 4.8 5.8 1.0 C A:TYR48 4.8 5.5 1.0 CB A:TYR48 4.8 5.7 1.0 CG A:TRP20 4.9 5.2 1.0

C.Koch, A.Heine, G.Klebe. Ligand-Induced Fit Affects Binding Modes and Provokes Changes in Crystal Packing of Aldose Reductase Biochim.Biophys.Acta V.1810 879 2011.
ISSN: ISSN 0006-3002
PubMed: 21684320
DOI: 10.1016/J.BBAGEN.2011.06.001