Zinc in PDB 7wsz: Human Glyoxalase I (with C-Ter His Tag) in Glycerol-Bound Form

All present enzymatic activity of Human Glyoxalase I (with C-Ter His Tag) in Glycerol-Bound Form:
4.4.1.5;

The structure of Human Glyoxalase I (with C-Ter His Tag) in Glycerol-Bound Form, PDB code: 7wsz was solved by M.Usami, K.Ando, H.Yokoyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.90 / 1.52
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	85.225, 96.995, 46.264, 90, 90, 90
R / Rfree (%)	16.1 / 18.7

The binding sites of Zinc atom in the Human Glyoxalase I (with C-Ter His Tag) in Glycerol-Bound Form (pdb code 7wsz). 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 (with C-Ter His Tag) in Glycerol-Bound Form, PDB code: 7wsz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Glyoxalase I (with C-Ter His Tag) in Glycerol-Bound Form


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 C-Ter His Tag) in Glycerol-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:23.4 occ:1.00 NE2 A:HIS126 2.0 17.1 1.0 OE1 B:GLU99 2.1 23.6 1.0 OE1 B:GLN33 2.1 21.0 1.0 OE1 A:GLU172 2.1 23.0 1.0 O2 A:GOL202 2.1 23.2 1.0 O3 A:GOL202 2.4 28.6 1.0 C2 A:GOL202 2.9 29.7 1.0 CE1 A:HIS126 3.0 17.4 1.0 CD B:GLU99 3.0 24.2 1.0 CD B:GLN33 3.1 19.0 1.0 CD2 A:HIS126 3.1 17.0 1.0 CD A:GLU172 3.1 21.5 1.0 C3 A:GOL202 3.1 33.5 1.0 OE2 B:GLU99 3.3 26.9 1.0 NE2 B:GLN33 3.5 17.6 1.0 OE2 A:GLU172 3.5 24.5 1.0 ND1 A:HIS126 4.1 17.4 1.0 CG A:HIS126 4.2 15.9 1.0 CG A:GLU172 4.3 16.3 1.0 C1 A:GOL202 4.3 32.8 1.0 CG B:GLN33 4.4 15.8 1.0 CG B:GLU99 4.4 18.0 1.0 CB A:GLU172 4.4 15.8 1.0 CB B:MET35 4.6 16.4 1.0 O B:HOH373 4.7 25.7 1.0 CB B:GLU99 4.8 17.8 1.0 CG B:MET35 4.8 18.1 1.0 O1 A:GOL202 4.9 33.0 1.0 CZ A:PHE162 5.0 22.4 1.0 CE2 A:PHE162 5.0 21.1 1.0

Zinc binding site 2 out of 2 in the Human Glyoxalase I (with C-Ter His Tag) in Glycerol-Bound Form


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 C-Ter His Tag) in Glycerol-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:23.8 occ:1.00 OE1 A:GLN33 2.0 22.9 1.0 NE2 B:HIS126 2.1 19.6 1.0 O A:HOH331 2.1 24.5 1.0 OE1 A:GLU99 2.1 28.5 1.0 OE1 B:GLU172 2.1 24.8 1.0 O B:HOH308 2.5 30.6 1.0 CE1 B:HIS126 3.0 20.2 1.0 CD A:GLU99 3.0 25.6 1.0 CD A:GLN33 3.0 20.9 1.0 CD B:GLU172 3.1 22.9 1.0 CD2 B:HIS126 3.1 19.8 1.0 OE2 A:GLU99 3.3 33.4 1.0 NE2 A:GLN33 3.4 19.8 1.0 OE2 B:GLU172 3.5 28.1 1.0 ND1 B:HIS126 4.1 18.2 1.0 CG B:HIS126 4.2 17.2 1.0 CG B:GLU172 4.3 20.0 1.0 CG A:GLN33 4.3 17.3 1.0 CG A:GLU99 4.4 19.3 1.0 CB B:GLU172 4.4 17.5 1.0 O A:HOH383 4.6 31.7 1.0 CB A:MET35 4.6 16.6 1.0 CB A:GLU99 4.8 18.7 1.0 CG A:MET35 4.8 19.2 1.0 CZ B:PHE162 5.0 23.0 1.0

M.Usami, K.Ando, A.Shibuya, R.Takasawa, H.Yokoyama. Crystal Structures of Human Glyoxalase I and Its Complex with TLSC702 Reveal Inhibitor Binding Mode and Substrate Preference. Febs Lett. V. 596 1458 2022.
ISSN: ISSN 0014-5793
PubMed: 35363883
DOI: 10.1002/1873-3468.14344