Zinc in PDB 7wt1: Human Glyoxalase I (with C-Ter His Tag) in Inhibitor-Free Form

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

The structure of Human Glyoxalase I (with C-Ter His Tag) in Inhibitor-Free Form, PDB code: 7wt1 was solved by M.Usami, A.Shibuya, H.Yokoyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.72 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.53, 65.221, 41.382, 90, 102.3, 90
R / Rfree (%)	19.3 / 23

The binding sites of Zinc atom in the Human Glyoxalase I (with C-Ter His Tag) in Inhibitor-Free Form (pdb code 7wt1). 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 Inhibitor-Free Form, PDB code: 7wt1:
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 Inhibitor-Free 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 Inhibitor-Free Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:36.5 occ:1.00 OE1 A:GLU172 2.1 35.0 1.0 OE1 B:GLU99 2.1 34.7 1.0 OE1 B:GLN33 2.1 38.1 1.0 NE2 A:HIS126 2.1 26.8 1.0 O B:HOH319 2.3 38.3 1.0 O A:HOH312 2.5 32.4 1.0 CD B:GLU99 3.1 38.8 1.0 CE1 A:HIS126 3.1 27.1 1.0 CD2 A:HIS126 3.1 25.7 1.0 CD B:GLN33 3.1 31.5 1.0 CD A:GLU172 3.1 37.4 1.0 OE2 B:GLU99 3.3 47.9 1.0 NE2 B:GLN33 3.6 28.9 1.0 OE2 A:GLU172 3.6 40.0 1.0 ND1 A:HIS126 4.2 29.2 1.0 CG A:HIS126 4.2 25.6 1.0 CG A:GLU172 4.4 30.0 1.0 CG B:GLU99 4.4 35.1 1.0 CG B:GLN33 4.4 28.0 1.0 CB A:GLU172 4.5 30.0 1.0 CB B:MET35 4.6 28.1 1.0 CG B:MET35 4.7 31.6 1.0 CB B:GLU99 4.8 30.4 1.0 CZ A:PHE162 4.9 33.9 1.0

Zinc binding site 2 out of 2 in the Human Glyoxalase I (with C-Ter His Tag) in Inhibitor-Free 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 Inhibitor-Free Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:39.5 occ:1.00 OE1 A:GLN33 2.1 36.3 1.0 OE1 B:GLU172 2.1 37.8 1.0 OE1 A:GLU99 2.1 33.2 1.0 NE2 B:HIS126 2.2 28.7 1.0 O B:HOH308 2.3 39.1 1.0 O A:HOH310 2.4 34.9 1.0 CD A:GLU99 3.1 39.5 1.0 CE1 B:HIS126 3.1 30.4 1.0 CD A:GLN33 3.1 32.4 1.0 CD B:GLU172 3.1 35.0 1.0 CD2 B:HIS126 3.2 30.7 1.0 OE2 A:GLU99 3.4 44.0 1.0 NE2 A:GLN33 3.5 30.4 1.0 OE2 B:GLU172 3.5 35.3 1.0 ND1 B:HIS126 4.2 29.7 1.0 CG B:HIS126 4.3 29.0 1.0 CG B:GLU172 4.4 32.6 1.0 CG A:GLN33 4.5 30.4 1.0 CG A:GLU99 4.5 36.8 1.0 CB B:GLU172 4.5 29.3 1.0 O B:HOH350 4.6 43.6 1.0 CB A:MET35 4.7 28.9 1.0 CG A:MET35 4.8 31.0 1.0 CB A:GLU99 4.9 32.8 1.0 O A:HOH327 5.0 45.9 1.0 CZ B:PHE162 5.0 34.4 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