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

Enzymatic activity of Human Glyoxalase I Q33E, E172Q Double Mutant

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

Protein crystallography data

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

Zinc Binding Sites:

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 1bh5

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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 1bh5

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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 1bh5

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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 1bh5

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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

Reference:

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
Page generated: Fri Sep 25 21:03:42 2020
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