Zinc in PDB 1fro: Human Glyoxalase I with Benzyl-Glutathione Inhibitor

All present enzymatic activity of Human Glyoxalase I with Benzyl-Glutathione Inhibitor:
4.4.1.5;

The structure of Human Glyoxalase I with Benzyl-Glutathione Inhibitor, PDB code: 1fro was solved by A.D.Cameron, T.A.Jones, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.50 / 2.20
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	68.000, 68.000, 169.400, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 23.4

The binding sites of Zinc atom in the Human Glyoxalase I with Benzyl-Glutathione Inhibitor (pdb code 1fro). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Human Glyoxalase I with Benzyl-Glutathione Inhibitor, PDB code: 1fro:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Human Glyoxalase I with Benzyl-Glutathione Inhibitor


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 with Benzyl-Glutathione Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:19.1 occ:1.00 OE1 B:GLU99 2.0 25.3 1.0 OE1 B:GLN33 2.0 15.6 1.0 OE1 A:GLU172 2.0 18.5 1.0 NE2 A:HIS126 2.0 10.4 1.0 O B:HOH202 2.1 24.7 1.0 CD B:GLU99 2.9 20.2 1.0 CD2 A:HIS126 3.0 10.3 1.0 CD A:GLU172 3.0 17.5 1.0 CE1 A:HIS126 3.0 8.3 1.0 OE2 B:GLU99 3.1 28.0 1.0 CD B:GLN33 3.1 15.1 1.0 OE2 A:GLU172 3.5 21.9 1.0 NE2 B:GLN33 3.6 18.0 1.0 ND1 A:HIS126 4.1 11.2 1.0 CG A:HIS126 4.1 11.1 1.0 CG A:GLU172 4.2 14.2 1.0 CG B:GLU99 4.3 15.1 1.0 CB B:MET35 4.3 10.0 1.0 CB A:GLU172 4.3 11.4 1.0 O A:HOH213 4.3 21.2 1.0 CG B:GLN33 4.4 13.1 1.0 CG B:MET35 4.5 11.1 1.0 CB B:GLU99 4.7 12.4 1.0 C2' A:GSB200 4.8 46.0 1.0 C3' A:GSB200 4.9 46.3 1.0

Zinc binding site 2 out of 4 in the Human Glyoxalase I with Benzyl-Glutathione Inhibitor


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 with Benzyl-Glutathione Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:19.1 occ:1.00 OE1 A:GLU99 2.0 25.3 1.0 OE1 A:GLN33 2.0 15.6 1.0 OE1 B:GLU172 2.0 18.5 1.0 NE2 B:HIS126 2.0 10.4 1.0 O A:HOH202 2.1 24.7 1.0 CD A:GLU99 2.8 20.2 1.0 CD2 B:HIS126 3.0 10.3 1.0 CD B:GLU172 3.0 17.5 1.0 CE1 B:HIS126 3.0 8.3 1.0 OE2 A:GLU99 3.0 28.0 1.0 CD A:GLN33 3.1 15.1 1.0 OE2 B:GLU172 3.5 21.9 1.0 NE2 A:GLN33 3.6 18.0 1.0 ND1 B:HIS126 4.1 11.2 1.0 CG B:HIS126 4.1 11.1 1.0 CG A:GLU99 4.2 15.1 1.0 CG B:GLU172 4.2 14.2 1.0 CB A:MET35 4.3 10.0 1.0 CB B:GLU172 4.3 11.4 1.0 O B:HOH213 4.3 21.2 1.0 CG A:GLN33 4.4 13.1 1.0 CG A:MET35 4.5 11.1 1.0 CB A:GLU99 4.7 12.4 1.0 C2' B:GSB200 4.8 46.0 1.0 C3' B:GSB200 4.9 46.3 1.0

Zinc binding site 3 out of 4 in the Human Glyoxalase I with Benzyl-Glutathione Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Glyoxalase I with Benzyl-Glutathione Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:19.1 occ:1.00 OE1 D:GLU99 2.0 25.3 1.0 OE1 D:GLN33 2.0 15.6 1.0 OE1 C:GLU172 2.0 18.5 1.0 NE2 C:HIS126 2.0 10.4 1.0 O D:HOH254 2.1 24.7 1.0 CD D:GLU99 2.9 20.2 1.0 CD2 C:HIS126 3.0 10.3 1.0 CD C:GLU172 3.0 17.5 1.0 CE1 C:HIS126 3.0 8.3 1.0 OE2 D:GLU99 3.1 28.0 1.0 CD D:GLN33 3.1 15.1 1.0 OE2 C:GLU172 3.5 21.9 1.0 NE2 D:GLN33 3.6 18.0 1.0 ND1 C:HIS126 4.1 11.2 1.0 CG C:HIS126 4.1 11.1 1.0 CG C:GLU172 4.2 14.2 1.0 CG D:GLU99 4.3 15.1 1.0 CB D:MET35 4.3 10.0 1.0 CB C:GLU172 4.3 11.4 1.0 O C:HOH213 4.3 21.2 1.0 CG D:GLN33 4.4 13.1 1.0 CG D:MET35 4.5 11.1 1.0 CB D:GLU99 4.7 12.4 1.0 C2' C:GSB200 4.8 46.0 1.0 C3' C:GSB200 4.9 46.3 1.0

Zinc binding site 4 out of 4 in the Human Glyoxalase I with Benzyl-Glutathione Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Glyoxalase I with Benzyl-Glutathione Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:19.1 occ:1.00 OE1 C:GLU99 2.0 25.3 1.0 OE1 C:GLN33 2.0 15.6 1.0 OE1 D:GLU172 2.0 18.5 1.0 NE2 D:HIS126 2.0 10.4 1.0 O C:HOH202 2.1 24.7 1.0 CD C:GLU99 2.8 20.2 1.0 CD2 D:HIS126 3.0 10.3 1.0 CD D:GLU172 3.0 17.5 1.0 CE1 D:HIS126 3.0 8.3 1.0 OE2 C:GLU99 3.0 28.0 1.0 CD C:GLN33 3.1 15.1 1.0 OE2 D:GLU172 3.5 21.9 1.0 NE2 C:GLN33 3.6 18.0 1.0 ND1 D:HIS126 4.1 11.2 1.0 CG D:HIS126 4.1 11.1 1.0 CG C:GLU99 4.2 15.1 1.0 CG D:GLU172 4.2 14.2 1.0 CB C:MET35 4.3 10.0 1.0 CB D:GLU172 4.3 11.4 1.0 O D:HOH252 4.3 21.2 1.0 CG C:GLN33 4.4 13.1 1.0 CG C:MET35 4.5 11.1 1.0 CB C:GLU99 4.7 12.4 1.0 C2' D:GSB200 4.8 46.0 1.0 C3' D:GSB200 4.9 46.3 1.0

A.D.Cameron, B.Olin, M.Ridderstrom, B.Mannervik, T.A.Jones. Crystal Structure of Human Glyoxalase I--Evidence For Gene Duplication and 3D Domain Swapping. Embo J. V. 16 3386 1997.
ISSN: ISSN 0261-4189
PubMed: 9218781
DOI: 10.1093/EMBOJ/16.12.3386