Iodine in PDB 1qin: Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione

All present enzymatic activity of Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione:
4.4.1.5;

The structure of Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione, PDB code: 1qin was solved by A.D.Cameron, M.Ridderstrom, B.Olin, B.Mannervik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.700, 54.500, 78.900, 90.00, 98.20, 90.00
R / Rfree (%)	17.8 / 21

The structure of Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iodine atom in the Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione (pdb code 1qin). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 2 binding sites of Iodine where determined in the Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione, PDB code: 1qin:
Jump to Iodine binding site number: 1; 2;

Iodine binding site 1 out of 2 in the Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione within 5.0Å range: probe atom residue distance (Å) B Occ A:I300 b:27.6 occ:1.00 I A:GIP300 0.0 27.6 1.0 CZ A:GIP300 2.1 23.5 1.0 CM2 A:GIP300 3.0 22.0 1.0 CM1 A:GIP300 3.1 23.2 1.0 CE A:MET183 3.5 44.3 1.0 O A:MET179 4.0 36.8 1.0 CB A:MET179 4.2 44.5 1.0 CD1 B:LEU92 4.3 29.4 1.0 CL2 A:GIP300 4.3 20.5 1.0 CL1 A:GIP300 4.4 23.1 1.0 CZ B:PHE62 4.4 26.4 1.0 SG B:CYS60 4.4 28.9 1.0 CB A:LEU182 4.4 35.9 1.0 CD1 A:LEU182 4.4 34.8 1.0 CG2 B:ILE88 4.6 37.4 1.0 C A:MET179 4.8 37.9 1.0 SD A:MET183 4.8 52.6 1.0 CG2 A:GIP300 4.9 20.1 1.0 CG A:MET179 5.0 50.5 1.0 CG A:MET183 5.0 47.0 1.0 CA A:MET179 5.0 38.3 1.0

Iodine binding site 2 out of 2 in the Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione within 5.0Å range: probe atom residue distance (Å) B Occ B:I400 b:32.9 occ:1.00 I B:GIP400 0.0 32.9 1.0 CZ B:GIP400 2.2 23.5 1.0 CM1 B:GIP400 3.0 23.3 1.0 CM2 B:GIP400 3.1 22.6 1.0 CE B:MET183 3.5 48.7 0.0 O B:MET179 3.8 37.4 1.0 CB B:MET179 4.1 44.6 1.0 CB B:LEU182 4.3 36.2 1.0 CD1 A:LEU92 4.3 29.5 1.0 CL1 B:GIP400 4.4 23.4 1.0 CD1 B:LEU182 4.4 34.9 1.0 CL2 B:GIP400 4.4 21.0 1.0 CZ A:PHE62 4.4 26.4 1.0 SG A:CYS60 4.5 28.6 1.0 C B:MET179 4.6 38.2 1.0 CG2 A:ILE88 4.6 37.4 1.0 SD B:MET183 4.7 56.8 0.0 CA B:MET179 4.8 38.3 1.0 CG B:MET179 4.8 50.5 1.0 SD B:MET179 4.9 56.0 1.0 CG2 B:GIP400 4.9 20.3 1.0 CG B:LEU182 5.0 36.9 1.0 CG B:MET183 5.0 48.7 0.0

A.D.Cameron, M.Ridderstrom, B.Olin, M.J.Kavarana, D.J.Creighton, B.Mannervik. Reaction Mechanism of Glyoxalase I Explored By An X-Ray Crystallographic Analysis of the Human Enzyme in Complex with A Transition State Analogue. Biochemistry V. 38 13480 1999.
ISSN: ISSN 0006-2960
PubMed: 10521255
DOI: 10.1021/BI990696C