Atomistry » Zinc » PDB 1qmu-1r23 » 1qv7
Atomistry »
  Zinc »
    PDB 1qmu-1r23 »
      1qv7 »

Zinc in PDB 1qv7: Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol

Enzymatic activity of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol:
1.1.1.1;

Protein crystallography data

The structure of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol, PDB code: 1qv7 was solved by L.A.Lebrun, D.-H.Park, S.Ramaswamy, B.V.Plapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 44.050, 50.962, 92.466, 91.61, 103.03, 109.86
R / Rfree (%) 17.7 / 22.2

Other elements in 1qv7:

The structure of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol (pdb code 1qv7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol, PDB code: 1qv7:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1qv7

Go back to Zinc Binding Sites List in 1qv7
Zinc binding site 1 out of 4 in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn375

b:34.5
occ:1.00
 NE2 A:HIS67 2.1 20.9 1.0
SG A:CYS174 2.2 21.8 1.0
O1 A:DFB378 2.2 30.6 1.0
SG A:CYS46 2.4 29.8 1.0
CD2 A:HIS67 3.1 18.6 1.0
CE1 A:HIS67 3.1 21.5 1.0
C7 A:DFB378 3.1 34.1 1.0
CB A:CYS174 3.3 17.5 1.0
CB A:CYS46 3.3 24.7 1.0
C5N A:NAD377 3.4 19.0 1.0
C6N A:NAD377 4.0 18.2 1.0
C4N A:NAD377 4.2 16.3 1.0
ND1 A:HIS67 4.2 17.3 1.0
CG A:HIS67 4.2 17.4 1.0
OG A:SER48 4.2 24.1 1.0
CB A:SER48 4.3 22.5 1.0
C1 A:DFB378 4.5 34.4 1.0
NH2 A:ARG369 4.5 36.7 1.0
CA A:CYS174 4.6 16.7 1.0
CE2 A:PHE93 4.8 12.5 1.0
CA A:CYS46 4.8 23.6 1.0
N A:GLY175 4.8 15.2 1.0
OE2 A:GLU68 4.8 24.0 1.0
C A:CYS174 4.9 15.4 1.0

Zinc binding site 2 out of 4 in 1qv7

Go back to Zinc Binding Sites List in 1qv7
Zinc binding site 2 out of 4 in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn376

b:18.3
occ:1.00
 SG A:CYS103 2.3 16.9 1.0
SG A:CYS97 2.3 18.3 1.0
SG A:CYS111 2.3 15.8 1.0
SG A:CYS100 2.4 19.2 1.0
CB A:CYS111 3.3 17.1 1.0
CB A:CYS103 3.4 15.2 1.0
CB A:CYS97 3.4 19.4 1.0
CB A:CYS100 3.5 19.0 1.0
N A:CYS97 3.6 15.2 1.0
CA A:CYS111 3.7 16.5 1.0
N A:CYS100 3.9 20.4 1.0
N A:GLY98 3.9 18.1 1.0
CA A:CYS97 3.9 18.4 1.0
N A:LEU112 4.0 15.9 1.0
N A:CYS103 4.1 16.5 1.0
CA A:CYS100 4.2 19.9 1.0
C A:CYS97 4.3 19.4 1.0
C A:CYS111 4.3 17.4 1.0
CA A:CYS103 4.3 16.2 1.0
N A:LYS99 4.5 22.2 1.0
C A:GLN96 4.6 17.0 1.0
N A:LYS113 4.8 17.9 1.0
C A:CYS100 4.8 17.6 1.0
CA A:GLN96 4.9 16.0 1.0
CG A:LYS113 4.9 23.5 1.0
CA A:GLY98 4.9 20.5 1.0
O A:CYS100 4.9 16.9 1.0

Zinc binding site 3 out of 4 in 1qv7

Go back to Zinc Binding Sites List in 1qv7
Zinc binding site 3 out of 4 in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn375

b:37.3
occ:1.00
 NE2 B:HIS67 2.1 24.5 1.0
SG B:CYS174 2.2 26.3 1.0
O1 B:DFB378 2.3 33.3 1.0
SG B:CYS46 2.4 34.4 1.0
CD2 B:HIS67 3.0 25.1 1.0
CE1 B:HIS67 3.1 23.1 1.0
C7 B:DFB378 3.2 40.2 1.0
CB B:CYS46 3.3 28.6 1.0
CB B:CYS174 3.3 21.0 1.0
C5N B:NAD377 3.4 24.2 1.0
C6N B:NAD377 4.1 23.7 1.0
ND1 B:HIS67 4.2 22.4 1.0
CG B:HIS67 4.2 20.7 1.0
CB B:SER48 4.2 25.5 1.0
C4N B:NAD377 4.2 23.2 1.0
OG B:SER48 4.2 27.5 1.0
NH2 B:ARG369 4.5 35.5 1.0
C1 B:DFB378 4.6 42.0 1.0
CA B:CYS174 4.6 20.3 1.0
CA B:CYS46 4.8 28.4 1.0
N B:GLY175 4.8 19.5 1.0
OE2 B:GLU68 4.9 30.9 1.0
CE2 B:PHE93 4.9 19.7 1.0
C B:CYS174 5.0 20.4 1.0

Zinc binding site 4 out of 4 in 1qv7

Go back to Zinc Binding Sites List in 1qv7
Zinc binding site 4 out of 4 in the Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Horse Liver Alcohol Dehydrogenase HIS51GLN/LYS228ARG Mutant Complexed with Nad+ and 2,3-Difluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn376

b:22.1
occ:1.00
 SG B:CYS103 2.3 20.6 1.0
SG B:CYS97 2.3 23.7 1.0
SG B:CYS100 2.4 20.5 1.0
SG B:CYS111 2.4 20.2 1.0
CB B:CYS111 3.2 18.5 1.0
CB B:CYS103 3.3 19.1 1.0
CB B:CYS97 3.4 25.2 1.0
CB B:CYS100 3.4 23.2 1.0
N B:CYS97 3.5 23.3 1.0
CA B:CYS111 3.7 18.6 1.0
N B:CYS100 3.9 24.5 1.0
CA B:CYS97 3.9 24.3 1.0
N B:GLY98 3.9 25.7 1.0
N B:LEU112 3.9 19.4 1.0
CA B:CYS100 4.2 23.1 1.0
C B:CYS111 4.2 18.7 1.0
N B:CYS103 4.2 19.6 1.0
C B:CYS97 4.3 26.0 1.0
CA B:CYS103 4.3 19.4 1.0
N B:LYS99 4.4 25.9 1.0
C B:GLN96 4.6 21.9 1.0
C B:CYS100 4.8 22.6 1.0
N B:LYS113 4.9 20.9 1.0
CA B:GLY98 4.9 25.7 1.0
CA B:GLN96 4.9 21.1 1.0
CG B:LYS113 4.9 25.7 1.0
O B:CYS100 4.9 19.9 1.0

Reference:

L.A.Lebrun, D.-H.Park, S.Ramaswamy, B.V.Plapp. Participation of Histidine-51 in Catalysis By Horse Liver Alcohol Dehydrogenase. Biochemistry V. 43 3014 2004.
ISSN: ISSN 0006-2960
PubMed: 15023053
DOI: 10.1021/BI036103M
Page generated: Wed Oct 16 18:16:13 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy