Atomistry » Zinc » PDB 1q63-1qlj » 1qh5
Atomistry »
  Zinc »
    PDB 1q63-1qlj »
      1qh5 »

Zinc in PDB 1qh5: Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione

Enzymatic activity of Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione

All present enzymatic activity of Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione:
3.1.2.6;

Protein crystallography data

The structure of Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione, PDB code: 1qh5 was solved by A.D.Cameron, M.Ridderstrom, B.Olin, B.Mannervik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.550, 73.800, 164.700, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 23.2

Other elements in 1qh5:

The structure of Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione also contains other interesting chemical elements:

Bromine (Br) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione (pdb code 1qh5). 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 II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione, PDB code: 1qh5:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1qh5

Go back to Zinc Binding Sites List in 1qh5
Zinc binding site 1 out of 4 in the Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn261

b:17.5
occ:1.00
 O A:HOH464 2.0 25.0 1.0
NE2 A:HIS110 2.1 15.2 1.0
NE2 A:HIS54 2.1 12.8 1.0
ND1 A:HIS56 2.2 16.8 1.0
O A:HOH465 2.5 35.9 1.0
OD2 A:ASP134 2.6 16.6 1.0
CE1 A:HIS56 3.1 17.0 1.0
CD2 A:HIS54 3.1 14.5 1.0
CD2 A:HIS110 3.1 15.0 1.0
CE1 A:HIS110 3.2 15.9 1.0
CE1 A:HIS54 3.2 14.9 1.0
CG A:HIS56 3.3 13.8 1.0
ZN A:ZN262 3.5 16.9 1.0
CG A:ASP134 3.5 14.8 1.0
CB A:HIS56 3.6 14.5 1.0
CB A:ASP134 3.8 13.6 1.0
NE2 A:HIS59 4.1 14.1 1.0
CD2 A:HIS59 4.2 14.3 1.0
SG2 A:GSH463 4.3 31.2 1.0
NE2 A:HIS56 4.3 17.8 1.0
CG A:HIS110 4.3 15.6 1.0
ND1 A:HIS54 4.3 13.7 1.0
CG A:HIS54 4.3 14.5 1.0
ND1 A:HIS110 4.3 15.1 1.0
CD2 A:HIS56 4.4 14.3 1.0
OD1 A:ASP58 4.5 16.1 1.0
OD1 A:ASP134 4.6 16.6 1.0
CB2 A:GSH463 4.6 28.5 1.0
O A:HOH601 4.7 37.8 1.0
OD2 A:ASP58 4.9 17.2 1.0

Zinc binding site 2 out of 4 in 1qh5

Go back to Zinc Binding Sites List in 1qh5
Zinc binding site 2 out of 4 in the Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:16.9
occ:1.00
 OD2 A:ASP134 2.1 16.6 1.0
NE2 A:HIS59 2.1 14.1 1.0
NE2 A:HIS173 2.1 17.4 1.0
O A:HOH464 2.1 25.0 1.0
OD2 A:ASP58 2.3 17.2 1.0
SG2 A:GSH463 2.8 31.2 1.0
CG A:ASP134 3.0 14.8 1.0
CD2 A:HIS59 3.0 14.3 1.0
CE1 A:HIS173 3.1 17.8 1.0
CD2 A:HIS173 3.1 17.6 1.0
CE1 A:HIS59 3.2 14.7 1.0
OD1 A:ASP134 3.2 16.6 1.0
CG A:ASP58 3.3 13.5 1.0
ZN A:ZN261 3.5 17.5 1.0
OD1 A:ASP58 3.6 16.1 1.0
CB2 A:GSH463 3.7 28.5 1.0
ND2 A:ASN12 4.1 17.4 1.0
O A:HOH465 4.1 35.9 1.0
ND1 A:HIS59 4.2 14.5 1.0
CG A:HIS59 4.2 15.1 1.0
ND1 A:HIS173 4.3 18.6 1.0
CG A:HIS173 4.3 17.0 1.0
NE2 A:HIS54 4.3 12.8 1.0
CE1 A:HIS54 4.4 14.9 1.0
CB A:ASP134 4.4 13.6 1.0
CB A:ASP58 4.6 16.0 1.0

Zinc binding site 3 out of 4 in 1qh5

Go back to Zinc Binding Sites List in 1qh5
Zinc binding site 3 out of 4 in the Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn261

b:14.7
occ:1.00
 O B:HOH466 2.0 16.9 1.0
NE2 B:HIS54 2.1 12.3 1.0
NE2 B:HIS110 2.1 12.1 1.0
ND1 B:HIS56 2.2 13.7 1.0
OD2 B:ASP134 2.6 13.1 1.0
CD2 B:HIS54 3.1 10.5 1.0
CD2 B:HIS110 3.1 11.4 1.0
CE1 B:HIS56 3.1 15.3 1.0
CE1 B:HIS110 3.2 12.0 1.0
CE1 B:HIS54 3.2 12.8 1.0
CG B:HIS56 3.3 14.9 1.0
OZ1 B:GBP464 3.3 33.6 1.0
ZN B:ZN262 3.3 14.6 1.0
CG B:ASP134 3.5 11.9 1.0
CB B:HIS56 3.6 15.8 1.0
CD2 B:GBP464 3.8 31.8 1.0
CB B:ASP134 3.8 12.4 1.0
NE2 B:HIS59 4.0 12.6 1.0
CD2 B:HIS59 4.1 12.6 1.0
ND1 B:HIS110 4.3 12.3 1.0
CG B:HIS110 4.3 12.6 1.0
CG B:HIS54 4.3 11.4 1.0
ND1 B:HIS54 4.3 11.9 1.0
NE2 B:GBP464 4.3 35.2 1.0
NE2 B:HIS56 4.3 15.8 1.0
CD2 B:HIS56 4.4 14.8 1.0
SG2 B:GBP464 4.4 28.0 1.0
OD1 B:ASP58 4.5 15.1 1.0
OD1 B:ASP134 4.6 12.8 1.0
CG2 B:GBP464 4.6 35.6 1.0
CB2 B:GBP464 4.7 24.3 1.0
OD2 B:ASP58 4.8 14.7 1.0
CL1 B:GBP464 5.0 36.7 1.0

Zinc binding site 4 out of 4 in 1qh5

Go back to Zinc Binding Sites List in 1qh5
Zinc binding site 4 out of 4 in the Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Glyoxalase II with S-(N-Hydroxy-N-Bromophenylcarbamoyl) Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn262

b:14.6
occ:1.00
 O B:HOH466 2.0 16.9 1.0
NE2 B:HIS59 2.1 12.6 1.0
OD2 B:ASP134 2.1 13.1 1.0
NE2 B:HIS173 2.1 14.3 1.0
OD2 B:ASP58 2.3 14.7 1.0
CD2 B:HIS59 3.0 12.6 1.0
CG B:ASP134 3.0 11.9 1.0
CE1 B:HIS173 3.1 16.1 1.0
CD2 B:HIS173 3.1 11.7 1.0
CE1 B:HIS59 3.1 12.2 1.0
CG B:ASP58 3.2 15.1 1.0
OD1 B:ASP134 3.3 12.8 1.0
SG2 B:GBP464 3.3 28.0 1.0
ZN B:ZN261 3.3 14.7 1.0
OD1 B:ASP58 3.5 15.1 1.0
CB2 B:GBP464 3.9 24.3 1.0
CD2 B:GBP464 4.0 31.8 1.0
ND2 B:ASN12 4.1 15.1 1.0
NE2 B:HIS54 4.2 12.3 1.0
CG B:HIS59 4.2 11.8 1.0
ND1 B:HIS59 4.2 12.1 1.0
ND1 B:HIS173 4.3 13.5 1.0
CE1 B:HIS54 4.3 12.8 1.0
CG B:HIS173 4.3 12.1 1.0
OZ1 B:GBP464 4.4 33.6 1.0
CB B:ASP134 4.4 12.4 1.0
CB B:ASP58 4.6 16.1 1.0
NE2 B:GBP464 4.6 35.2 1.0
OF2 B:GBP464 4.7 37.3 1.0
NE2 B:HIS110 4.9 12.1 1.0

Reference:

A.D.Cameron, M.Ridderstrom, B.Olin, B.Mannervik. Crystal Structure of Human Glyoxalase II and Its Complex with A Glutathione Thiolester Substrate Analogue. Structure Fold.Des. V. 7 1067 1999.
ISSN: ISSN 0969-2126
PubMed: 10508780
DOI: 10.1016/S0969-2126(99)80174-9
Page generated: Wed Oct 16 18:09:22 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy