Zinc 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:

Iodine

(I)

2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Glyoxalase I Complexed with S-(N-Hydroxy-N-P- Iodophenylcarbamoyl) Glutathione, PDB code: 1qin:
Jump to Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn401 b:18.5 occ:1.00 OE1 A:GLU99 1.9 17.7 1.0 OF2 B:GIP400 2.0 17.9 1.0 NE2 B:HIS126 2.0 13.0 1.0 OE1 A:GLN33 2.1 17.2 1.0 OZ1 B:GIP400 2.1 17.8 1.0 NE2 B:GIP400 2.7 18.4 1.0 CD2 B:GIP400 2.7 18.2 1.0 CD A:GLU99 2.8 19.2 1.0 OE2 A:GLU99 3.0 22.5 1.0 CE1 B:HIS126 3.0 12.7 1.0 CD2 B:HIS126 3.0 13.0 1.0 CD A:GLN33 3.1 15.6 1.0 OE1 B:GLU172 3.2 21.2 1.0 NE2 A:GLN33 3.6 15.2 1.0 CD B:GLU172 3.9 23.8 1.0 CG2 B:GIP400 4.1 20.3 1.0 ND1 B:HIS126 4.2 13.6 1.0 O A:HOH406 4.2 15.6 1.0 OE2 B:GLU172 4.2 28.3 1.0 CG B:HIS126 4.2 13.5 1.0 CG A:GLU99 4.2 16.5 1.0 CB A:MET35 4.3 14.1 1.0 CG A:GLN33 4.4 14.0 1.0 SG2 B:GIP400 4.5 19.6 1.0 CG A:MET35 4.5 13.7 1.0 CB A:GLU99 4.7 13.9 1.0 CL2 B:GIP400 4.7 21.0 1.0 CB B:GLU172 5.0 18.8 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn301 b:18.3 occ:1.00 OE1 B:GLU99 1.9 17.6 1.0 OE1 B:GLN33 2.0 17.4 1.0 OF2 A:GIP300 2.1 17.6 1.0 NE2 A:HIS126 2.1 12.9 1.0 OZ1 A:GIP300 2.1 17.9 1.0 NE2 A:GIP300 2.7 18.6 1.0 CD2 A:GIP300 2.7 18.4 1.0 CD B:GLU99 2.8 19.0 1.0 OE2 B:GLU99 3.0 22.9 1.0 CE1 A:HIS126 3.0 12.6 1.0 CD B:GLN33 3.1 16.1 1.0 CD2 A:HIS126 3.1 13.0 1.0 OE1 A:GLU172 3.3 21.1 1.0 NE2 B:GLN33 3.6 15.2 1.0 CD A:GLU172 4.0 23.6 1.0 CG2 A:GIP300 4.1 20.1 1.0 ND1 A:HIS126 4.2 13.6 1.0 O A:HOH404 4.2 18.9 1.0 CG B:GLU99 4.2 16.5 1.0 CG A:HIS126 4.2 13.6 1.0 OE2 A:GLU172 4.3 27.9 1.0 CB B:MET35 4.3 14.2 1.0 CG B:GLN33 4.4 14.0 1.0 CG B:MET35 4.5 13.9 1.0 SG2 A:GIP300 4.5 20.1 1.0 CB B:GLU99 4.6 13.9 1.0 CL2 A:GIP300 4.7 20.5 1.0 CB A:GLU172 5.0 18.7 1.0

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