Zinc in PDB 1bh5: Human Glyoxalase I Q33E, E172Q Double Mutant

All present enzymatic activity of Human Glyoxalase I Q33E, E172Q Double Mutant:
4.4.1.5;

The structure of Human Glyoxalase I Q33E, E172Q Double Mutant, PDB code: 1bh5 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)	30.00 / 2.20
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	67.280, 67.280, 164.730, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 25

The binding sites of Zinc atom in the Human Glyoxalase I Q33E, E172Q Double Mutant (pdb code 1bh5). 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 Q33E, E172Q Double Mutant, PDB code: 1bh5:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Human Glyoxalase I Q33E, E172Q Double Mutant


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 Q33E, E172Q Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:17.3 occ:1.00 NE2 A:HIS126 2.0 8.5 1.0 OE1 B:GLU99 2.0 13.8 1.0 OE2 B:GLU33 2.0 15.2 1.0 O B:HOH202 2.2 20.6 1.0 OE1 A:GLN172 2.9 14.4 1.0 CD B:GLU99 2.9 13.1 1.0 CE1 A:HIS126 2.9 10.0 1.0 CD B:GLU33 2.9 18.2 1.0 CD2 A:HIS126 3.1 9.4 1.0 OE2 B:GLU99 3.2 15.8 1.0 OE1 B:GLU33 3.2 12.5 1.0 O B:HOH203 3.3 29.6 1.0 CD A:GLN172 3.5 15.6 1.0 NE2 A:GLN172 3.7 12.9 1.0 O B:HOH245 4.0 14.9 1.0 ND1 A:HIS126 4.1 8.0 1.0 CG A:HIS126 4.2 9.4 1.0 CB B:MET35 4.3 11.4 1.0 CG B:GLU33 4.3 14.1 1.0 CG B:MET35 4.3 9.3 1.0 CG B:GLU99 4.3 11.3 1.0 CB A:GLN172 4.6 12.5 1.0 CG A:GLN172 4.7 15.0 1.0 CB B:GLU99 4.7 9.9 1.0

Zinc binding site 2 out of 4 in the Human Glyoxalase I Q33E, E172Q Double Mutant


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 Q33E, E172Q Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:20.6 occ:1.00 OE2 A:GLU33 2.0 15.2 1.0 NE2 B:HIS126 2.1 10.8 1.0 OE1 A:GLU99 2.1 12.9 1.0 O A:HOH202 2.4 31.6 1.0 OE1 B:GLN172 2.7 15.3 1.0 CD A:GLU33 2.9 17.9 1.0 CD A:GLU99 2.9 12.5 1.0 CE1 B:HIS126 2.9 9.6 1.0 OE2 A:GLU99 3.1 15.4 1.0 OE1 A:GLU33 3.1 11.9 1.0 CD2 B:HIS126 3.1 9.6 1.0 CD B:GLN172 3.2 12.9 1.0 NE2 B:GLN172 3.3 10.8 1.0 O A:HOH203 3.3 20.6 1.0 ND1 B:HIS126 4.1 9.6 1.0 CG B:HIS126 4.2 10.4 1.0 CB A:MET35 4.2 10.6 1.0 CG A:GLU33 4.3 15.6 1.0 O B:HOH209 4.3 14.1 1.0 CG A:GLU99 4.4 12.2 1.0 CG A:MET35 4.4 12.0 1.0 CG B:GLN172 4.5 12.1 1.0 CB B:GLN172 4.6 14.3 1.0 CB A:GLU99 4.8 7.6 1.0 CZ B:PHE162 4.9 14.4 1.0

Zinc binding site 3 out of 4 in the Human Glyoxalase I Q33E, E172Q Double Mutant


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 Q33E, E172Q Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:18.2 occ:1.00 O C:HOH202 1.8 20.6 1.0 NE2 C:HIS126 2.0 8.4 1.0 OE2 D:GLU33 2.1 15.3 1.0 OE1 D:GLU99 2.2 14.5 1.0 O D:HOH203 2.7 36.6 1.0 OE1 C:GLN172 2.7 14.6 1.0 CE1 C:HIS126 2.9 10.0 1.0 OE2 D:GLU99 2.9 13.7 1.0 CD D:GLU33 3.0 18.4 1.0 CD D:GLU99 3.0 9.9 1.0 CD2 C:HIS126 3.0 9.3 1.0 OE1 D:GLU33 3.3 12.4 1.0 CD C:GLN172 3.3 15.6 1.0 NE2 C:GLN172 3.5 12.7 1.0 ND1 C:HIS126 4.0 8.2 1.0 CG C:HIS126 4.1 9.5 1.0 CG D:GLU33 4.3 14.0 1.0 CB D:MET35 4.4 11.4 1.0 O C:HOH210 4.4 15.9 1.0 CG D:MET35 4.5 9.2 1.0 CG D:GLU99 4.5 9.9 1.0 CG C:GLN172 4.5 14.8 1.0 CB C:GLN172 4.5 12.7 1.0 CB D:GLU99 4.8 11.0 1.0

Zinc binding site 4 out of 4 in the Human Glyoxalase I Q33E, E172Q Double Mutant


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 Q33E, E172Q Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:20.4 occ:1.00 OE2 C:GLU33 2.0 15.4 1.0 OE1 C:GLU99 2.1 10.7 1.0 NE2 D:HIS126 2.2 11.0 1.0 O C:HOH203 2.4 10.8 1.0 OE1 D:GLN172 2.5 15.3 1.0 O C:HOH204 2.5 22.5 1.0 CD C:GLU33 2.8 18.0 1.0 CD C:GLU99 3.0 13.9 1.0 OE1 C:GLU33 3.0 12.0 1.0 CE1 D:HIS126 3.1 9.8 1.0 CD D:GLN172 3.1 13.3 1.0 CD2 D:HIS126 3.2 9.6 1.0 NE2 D:GLN172 3.2 10.6 1.0 OE2 C:GLU99 3.2 18.5 1.0 ND1 D:HIS126 4.2 9.9 1.0 CG C:GLU33 4.2 15.7 1.0 CG D:HIS126 4.3 10.7 1.0 CB C:MET35 4.3 10.9 1.0 CG D:GLN172 4.4 12.2 1.0 CG C:GLU99 4.4 13.4 1.0 CG C:MET35 4.4 11.9 1.0 CB D:GLN172 4.5 14.4 1.0 O C:HOH245 4.6 17.9 1.0 CB C:GLU99 4.8 6.9 1.0

M.Ridderstrom, A.D.Cameron, T.A.Jones, B.Mannervik. Involvement of An Active-Site ZN2+ Ligand in the Catalytic Mechanism of Human Glyoxalase I. J.Biol.Chem. V. 273 21623 1998.
ISSN: ISSN 0021-9258
PubMed: 9705294
DOI: 10.1074/JBC.273.34.21623