Chlorine in PDB 2pdu: Human Aldose Reductase Mutant C303D Complexed with IDD393.

All present enzymatic activity of Human Aldose Reductase Mutant C303D Complexed with IDD393.:
1.1.1.21;

The structure of Human Aldose Reductase Mutant C303D Complexed with IDD393., PDB code: 2pdu was solved by H.Steuber, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.55
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	40.130, 47.250, 47.340, 76.27, 67.37, 77.06
R / Rfree (%)	15.9 / 21.2

The binding sites of Chlorine atom in the Human Aldose Reductase Mutant C303D Complexed with IDD393. (pdb code 2pdu). 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 C303D Complexed with IDD393., PDB code: 2pdu:

Chlorine binding site 1 out of 1 in the Human Aldose Reductase Mutant C303D 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 C303D Complexed with IDD393. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl600 b:12.1 occ:1.00 CL1 A:393600 0.0 12.1 1.0 C13 A:393600 1.8 10.2 1.0 C12 A:393600 2.6 10.5 1.0 C15 A:393600 2.8 9.0 1.0 O A:VAL47 3.3 9.5 1.0 O A:HOH679 3.5 18.7 1.0 NE1 A:TRP20 3.5 8.9 1.0 O A:HOH643 3.6 14.1 1.0 CD1 A:TRP20 3.8 9.9 1.0 C11 A:393600 3.9 10.9 1.0 C A:VAL47 4.0 7.6 1.0 O A:HOH766 4.0 22.1 1.0 CD1 A:TYR48 4.0 6.7 1.0 O A:HOH818 4.0 30.9 1.0 CG2 A:VAL47 4.0 10.2 1.0 CG1 A:VAL47 4.1 9.3 1.0 C16 A:393600 4.1 10.1 1.0 CA A:TYR48 4.3 6.6 1.0 O A:HOH765 4.4 12.8 1.0 N A:TYR48 4.5 8.9 1.0 O A:HOH617 4.5 12.3 1.0 CB A:VAL47 4.5 11.8 1.0 CE1 A:TYR48 4.5 6.0 1.0 C10 A:393600 4.5 6.7 1.0 CE2 A:TRP20 4.6 6.8 1.0 CA A:VAL47 4.9 9.1 1.0 CG A:TRP20 4.9 7.6 1.0

H.Steuber, A.Heine, A.Podjarny, G.Klebe. Merging the Binding Sites of Aldose and Aldehyde Reductase For Detection of Inhibitor Selectivity-Determining Features. J.Mol.Biol. V. 379 991 2008.
ISSN: ISSN 0022-2836
PubMed: 18495158
DOI: 10.1016/J.JMB.2008.03.063