Bromine in PDB 3lep: Human Aldose Reductase Mutant T113C in Complex with IDD388

All present enzymatic activity of Human Aldose Reductase Mutant T113C in Complex with IDD388:
1.1.1.21;

The structure of Human Aldose Reductase Mutant T113C in Complex with IDD388, PDB code: 3lep 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)	10.00 / 0.99
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.270, 66.920, 47.340, 90.00, 92.26, 90.00
R / Rfree (%)	10.9 / 13

The structure of Human Aldose Reductase Mutant T113C in Complex with IDD388 also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Chlorine	(Cl)	1 atom

The binding sites of Bromine atom in the Human Aldose Reductase Mutant T113C in Complex with IDD388 (pdb code 3lep). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Human Aldose Reductase Mutant T113C in Complex with IDD388, PDB code: 3lep:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Human Aldose Reductase Mutant T113C in Complex with IDD388


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Human Aldose Reductase Mutant T113C in Complex with IDD388 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br600 b:7.6 occ:0.76 BR8 A:388600 0.0 7.6 0.8 C5 A:388600 1.9 6.0 1.0 BR A:BR700 2.0 25.6 0.2 C6 A:388600 2.8 6.4 1.0 C4 A:388600 2.9 5.8 1.0 SG A:CYS113 3.4 6.8 0.7 CB A:CYS113 3.7 5.2 0.7 CB A:CYS303 3.9 7.7 1.0 SG A:CYS113 3.9 20.8 0.3 CB A:CYS113 3.9 6.0 0.3 CZ A:PHE115 3.9 6.1 1.0 CB A:TRP111 4.0 4.4 1.0 CE3 A:TRP111 4.0 4.8 1.0 SG A:CYS303 4.1 7.8 1.0 C7 A:388600 4.1 5.5 1.0 CG A:TRP111 4.1 4.4 1.0 CD2 A:TRP111 4.1 4.4 1.0 C3 A:388600 4.2 5.2 1.0 CE1 A:PHE115 4.2 5.6 1.0 CD2 A:TYR309 4.4 6.3 1.0 C2 A:388600 4.7 4.8 1.0 CE2 A:TYR309 4.7 6.9 1.0 SG A:CYS80 4.8 4.4 1.0 CZ3 A:TRP111 4.8 5.4 1.0 CD1 A:TRP111 5.0 4.7 1.0

Bromine binding site 2 out of 2 in the Human Aldose Reductase Mutant T113C in Complex with IDD388


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Human Aldose Reductase Mutant T113C in Complex with IDD388 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br700 b:25.6 occ:0.24 BR8 A:388600 2.0 7.6 0.8 SG A:CYS113 2.3 6.8 0.7 SG A:CYS113 2.9 20.8 0.3 CB A:CYS113 3.2 5.2 0.7 CB A:CYS113 3.3 6.0 0.3 C5 A:388600 3.4 6.0 1.0 CD A:PRO310 3.5 5.1 1.0 CB A:TRP111 3.5 4.4 1.0 CE3 A:TRP111 3.5 4.8 1.0 N A:CYS113 3.9 6.4 1.0 C6 A:388600 3.9 6.4 1.0 CD A:PRO112 3.9 4.6 1.0 CD2 A:TRP111 4.0 4.4 1.0 CG A:TRP111 4.1 4.4 1.0 N A:PRO112 4.2 3.9 0.5 CG A:PRO112 4.2 5.2 1.0 CA A:CYS113 4.2 4.9 0.7 N A:PRO112 4.2 3.9 0.5 CA A:CYS113 4.2 4.8 0.3 CG A:PRO310 4.3 5.4 1.0 CD2 A:TYR309 4.4 6.3 1.0 CA A:TYR309 4.4 5.7 1.0 C4 A:388600 4.5 5.8 1.0 CZ3 A:TRP111 4.5 5.4 1.0 C A:PRO112 4.5 3.7 0.5 CA A:TRP111 4.5 3.7 1.0 C A:TRP111 4.6 3.6 1.0 O A:ASP308 4.6 5.6 1.0 N A:PRO310 4.7 5.1 1.0 C A:PRO112 4.8 4.4 0.5 CA A:PRO112 4.9 4.3 0.5 CA A:PRO112 5.0 4.4 0.5 N A:TYR309 5.0 5.8 1.0 CE2 A:TYR309 5.0 6.9 1.0

C.Koch, A.Heine, G.Klebe. Tracing the Detail: How Mutations Affect Binding Modes and Thermodynamic Signatures of Closely Related Aldose Reductase Inhibitors J.Mol.Biol. V. 406 700 2011.
ISSN: ISSN 0022-2836
PubMed: 21185307
DOI: 10.1016/J.JMB.2010.11.058