Atomistry » Zinc » PDB 3oke-3ox3 » 3oq6
Atomistry »
  Zinc »
    PDB 3oke-3ox3 »
      3oq6 »

Zinc in PDB 3oq6: Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol

Enzymatic activity of Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol:
1.1.1.1;

Protein crystallography data

The structure of Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol, PDB code: 3oq6 was solved by B.V.Plapp, T.J.Herdendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.85 / 1.20
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 44.340, 51.310, 92.210, 91.98, 102.95, 110.11
R / Rfree (%) 13.5 / 16.2

Other elements in 3oq6:

The structure of Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol also contains other interesting chemical elements:

Fluorine (F) 10 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol (pdb code 3oq6). 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 A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol, PDB code: 3oq6:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3oq6

Go back to Zinc Binding Sites List in 3oq6
Zinc binding site 1 out of 4 in the Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl 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 A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn375

b:10.6
occ:1.00
 O1 A:PFB378 1.9 10.5 1.0
NE2 A:HIS67 2.0 10.3 1.0
SG A:CYS46 2.3 10.1 1.0
SG A:CYS174 2.3 10.6 1.0
C7 A:PFB378 2.9 10.4 1.0
CE1 A:HIS67 3.0 8.9 1.0
CD2 A:HIS67 3.1 9.8 1.0
CB A:CYS46 3.3 10.2 1.0
C5N A:NAJ377 3.3 9.6 1.0
CB A:CYS46 3.3 11.0 0.0
CB A:CYS174 3.4 9.8 1.0
SG A:CYS46 3.5 10.6 0.0
OG A:SER48 3.8 10.0 1.0
C4N A:NAJ377 3.9 9.2 1.0
C6N A:NAJ377 3.9 8.9 1.0
CB A:SER48 4.0 9.8 1.0
F6 A:PFB378 4.1 12.5 1.0
ND1 A:HIS67 4.1 9.7 1.0
C1 A:PFB378 4.1 10.9 1.0
CG A:HIS67 4.2 9.6 1.0
C6 A:PFB378 4.6 12.2 1.0
NH2 A:ARG369 4.6 11.0 1.0
CA A:CYS174 4.8 9.3 1.0
CA A:CYS46 4.8 10.5 1.0
CE2 A:PHE93 4.8 10.7 1.0
N A:SER48 4.8 9.6 1.0
N1N A:NAJ377 4.9 8.6 1.0
OE2 A:GLU68 4.9 12.7 1.0
C3N A:NAJ377 5.0 9.1 1.0

Zinc binding site 2 out of 4 in 3oq6

Go back to Zinc Binding Sites List in 3oq6
Zinc binding site 2 out of 4 in the Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl 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 A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn376

b:11.3
occ:1.00
 SG A:CYS111 2.3 10.8 1.0
SG A:CYS103 2.3 11.1 1.0
SG A:CYS100 2.3 11.6 1.0
SG A:CYS97 2.4 12.8 1.0
CB A:CYS111 3.3 10.4 1.0
CB A:CYS103 3.4 10.4 1.0
CB A:CYS100 3.4 12.2 1.0
CB A:CYS97 3.4 12.9 1.0
N A:CYS97 3.5 11.3 1.0
CA A:CYS111 3.7 9.6 1.0
N A:CYS100 3.9 14.2 1.0
CA A:CYS97 3.9 12.1 1.0
N A:GLY98 4.0 12.9 1.0
N A:LEU112 4.0 10.4 1.0
N A:CYS103 4.2 11.1 1.0
CA A:CYS100 4.2 13.6 1.0
C A:CYS111 4.3 10.0 1.0
C A:CYS97 4.3 12.4 1.0
CA A:CYS103 4.4 10.6 1.0
N A:LYS99 4.5 14.8 1.0
C A:GLN96 4.6 11.2 1.0
N A:LYS113 4.8 10.6 1.0
C A:CYS100 4.9 13.1 1.0
CA A:GLN96 4.9 11.2 1.0
CG A:LYS113 4.9 15.9 1.0
O A:CYS100 4.9 12.5 1.0
O A:HOH552 5.0 29.1 1.0
CA A:GLY98 5.0 14.5 1.0

Zinc binding site 3 out of 4 in 3oq6

Go back to Zinc Binding Sites List in 3oq6
Zinc binding site 3 out of 4 in the Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl 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 A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn375

b:12.5
occ:1.00
 O1 B:PFB378 1.9 12.9 1.0
NE2 B:HIS67 2.0 12.1 1.0
SG B:CYS174 2.3 12.6 1.0
SG B:CYS46 2.3 12.3 1.0
C7 B:PFB378 2.9 13.2 1.0
CE1 B:HIS67 3.0 11.0 1.0
CD2 B:HIS67 3.0 10.8 1.0
CB B:CYS46 3.3 11.8 1.0
C5N B:NAJ377 3.3 10.6 1.0
CB B:CYS174 3.4 11.4 1.0
OG B:SER48 3.8 11.7 1.0
C4N B:NAJ377 3.9 11.7 1.0
CB B:SER48 4.0 11.6 1.0
C6N B:NAJ377 4.0 10.2 1.0
F6 B:PFB378 4.0 13.7 1.0
ND1 B:HIS67 4.1 11.7 1.0
C1 B:PFB378 4.2 13.4 1.0
CG B:HIS67 4.2 11.0 1.0
C6 B:PFB378 4.6 13.0 1.0
NH2 B:ARG369 4.6 13.4 1.0
CA B:CYS174 4.7 10.7 1.0
CA B:CYS46 4.8 11.9 1.0
N B:SER48 4.8 11.7 1.0
CE2 B:PHE93 4.8 12.4 1.0
N1N B:NAJ377 4.9 10.1 1.0
OE2 B:GLU68 4.9 13.8 1.0
C3N B:NAJ377 5.0 10.8 1.0

Zinc binding site 4 out of 4 in 3oq6

Go back to Zinc Binding Sites List in 3oq6
Zinc binding site 4 out of 4 in the Horse Liver Alcohol Dehydrogenase A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl 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 A317C Mutant Complexed with Nad+ and 2,3,4,5,6-Pentafluorobenzyl Alcohol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn376

b:13.9
occ:1.00
 SG B:CYS111 2.3 13.1 1.0
SG B:CYS97 2.3 17.0 1.0
SG B:CYS103 2.4 12.9 1.0
SG B:CYS100 2.4 14.4 1.0
CB B:CYS111 3.3 11.9 1.0
CB B:CYS103 3.4 13.0 1.0
CB B:CYS100 3.4 15.5 1.0
CB B:CYS97 3.4 15.4 1.0
N B:CYS97 3.5 13.8 1.0
CA B:CYS111 3.7 11.5 1.0
N B:CYS100 3.9 17.0 1.0
CA B:CYS97 3.9 14.5 1.0
N B:LEU112 3.9 12.3 1.0
N B:GLY98 3.9 15.4 1.0
CA B:CYS100 4.2 16.5 1.0
N B:CYS103 4.2 12.8 1.0
C B:CYS111 4.2 11.9 1.0
C B:CYS97 4.3 15.4 1.0
CA B:CYS103 4.4 12.4 1.0
N B:LYS99 4.5 17.6 1.0
C B:GLN96 4.6 12.8 1.0
N B:LYS113 4.8 13.0 1.0
C B:CYS100 4.8 16.3 1.0
CG B:LYS113 4.9 17.7 1.0
CA B:GLN96 4.9 12.3 1.0
O B:CYS100 4.9 15.3 1.0
CA B:GLY98 5.0 16.6 1.0
O B:HOH482 5.0 31.5 1.0

Reference:

T.J.Herdendorf, B.V.Plapp. Origins of the High Catalytic Activity of Human Alcohol Dehydrogenase 4 Studied with Horse Liver A317C Alcohol Dehydrogenase. Chem.Biol.Interact V. 191 42 2011.
ISSN: ISSN 0009-2797
PubMed: 21184752
DOI: 10.1016/J.CBI.2010.12.015
Page generated: Wed Dec 16 04:41:06 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy