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Zinc in PDB 1axe: Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol

Enzymatic activity of Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol

All present enzymatic activity of Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol:
1.1.1.1;

Protein crystallography data

The structure of Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol, PDB code: 1axe was solved by T.D.Colby, J.K.Chin, B.M.Goldstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 51.820, 44.580, 93.280, 103.10, 87.59, 70.55
R / Rfree (%) 20.3 / 26.9

Other elements in 1axe:

The structure of Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol also contains other interesting chemical elements:

Fluorine (F) 6 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol (pdb code 1axe). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol, PDB code: 1axe:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1axe

Go back to Zinc Binding Sites List in 1axe
Zinc binding site 1 out of 4 in the Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:23.6
occ:1.00
 O A:ETF404 2.1 22.8 1.0
NE2 A:HIS67 2.2 17.9 1.0
SG A:CYS46 2.2 15.9 1.0
SG A:CYS174 2.3 16.8 1.0
CE1 A:HIS67 3.0 11.7 1.0
C2 A:ETF404 3.2 26.8 1.0
CB A:CYS46 3.2 14.2 1.0
C5N A:NAD403 3.3 3.0 1.0
CD2 A:HIS67 3.4 15.2 1.0
OG A:SER48 3.6 18.1 1.0
CB A:CYS174 3.7 14.9 1.0
C6N A:NAD403 3.8 7.3 1.0
CB A:SER48 3.9 11.3 1.0
C4N A:NAD403 4.1 8.1 1.0
ND1 A:HIS67 4.2 14.0 1.0
C1 A:ETF404 4.4 28.1 1.0
CG A:HIS67 4.4 11.8 1.0
CA A:CYS46 4.7 13.6 1.0
F2 A:ETF404 4.7 27.5 1.0
NH2 A:ARG369 4.7 12.2 1.0
N A:SER48 4.8 10.0 1.0
F1 A:ETF404 4.9 32.2 1.0
N1N A:NAD403 4.9 5.5 1.0
CA A:SER48 5.0 11.6 1.0
OE1 A:GLU68 5.0 15.9 1.0

Zinc binding site 2 out of 4 in 1axe

Go back to Zinc Binding Sites List in 1axe
Zinc binding site 2 out of 4 in the Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:22.3
occ:1.00
 SG A:CYS111 2.0 14.1 1.0
SG A:CYS103 2.2 20.6 1.0
SG A:CYS97 2.3 23.2 1.0
SG A:CYS100 2.5 18.5 1.0
CB A:CYS111 3.4 14.1 1.0
CB A:CYS97 3.4 19.9 1.0
CB A:CYS103 3.6 18.0 1.0
CB A:CYS100 3.6 18.9 1.0
N A:CYS97 3.6 18.0 1.0
CA A:CYS111 3.9 15.5 1.0
CA A:CYS97 4.0 20.0 1.0
N A:GLY98 4.0 22.5 1.0
N A:CYS100 4.1 22.0 1.0
N A:LEU112 4.1 17.8 1.0
N A:CYS103 4.3 20.3 1.0
C A:CYS97 4.3 24.1 1.0
CA A:CYS100 4.4 20.4 1.0
C A:CYS111 4.5 14.6 1.0
CA A:CYS103 4.5 21.6 1.0
C A:GLN96 4.6 15.5 1.0
CG A:LYS113 4.7 23.3 1.0
N A:LYS99 4.7 23.6 1.0
CA A:GLN96 4.9 14.4 1.0
N A:LYS113 4.9 22.4 1.0
CA A:GLY98 4.9 21.8 1.0
C A:CYS100 5.0 20.5 1.0
O A:CYS100 5.0 23.0 1.0

Zinc binding site 3 out of 4 in 1axe

Go back to Zinc Binding Sites List in 1axe
Zinc binding site 3 out of 4 in the Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:25.0
occ:1.00
 O B:ETF404 2.1 23.8 1.0
NE2 B:HIS67 2.1 25.3 1.0
SG B:CYS174 2.1 20.0 1.0
SG B:CYS46 2.3 26.3 1.0
CE1 B:HIS67 3.0 21.1 1.0
C2 B:ETF404 3.2 31.0 1.0
CD2 B:HIS67 3.3 20.9 1.0
CB B:CYS46 3.3 27.5 1.0
C5N B:NAD403 3.4 12.9 1.0
CB B:CYS174 3.5 18.2 1.0
OG B:SER48 3.8 16.1 1.0
C6N B:NAD403 3.9 11.2 1.0
CB B:SER48 4.1 16.6 1.0
F2 B:ETF404 4.2 39.9 1.0
C4N B:NAD403 4.2 14.0 1.0
ND1 B:HIS67 4.2 21.7 1.0
C1 B:ETF404 4.2 34.9 1.0
CG B:HIS67 4.3 20.2 1.0
NH2 B:ARG369 4.7 25.2 1.0
CA B:CYS46 4.8 26.2 1.0
CA B:CYS174 4.9 18.2 1.0
N B:GLY175 4.9 19.8 1.0
F3 B:ETF404 4.9 38.0 1.0
N B:SER48 4.9 15.3 1.0

Zinc binding site 4 out of 4 in 1axe

Go back to Zinc Binding Sites List in 1axe
Zinc binding site 4 out of 4 in the Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the Active-Site Mutant PHE93->Trp of Horse Liver Alcohol Dehydrogenase in Complex with Nad and Inhibitor Trifluoroethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn402

b:22.2
occ:1.00
 SG B:CYS103 2.0 13.6 1.0
SG B:CYS111 2.3 16.2 1.0
SG B:CYS97 2.4 27.0 1.0
SG B:CYS100 2.4 16.3 1.0
CB B:CYS111 3.3 14.5 1.0
CB B:CYS103 3.4 19.0 1.0
CB B:CYS97 3.4 26.6 1.0
N B:CYS97 3.5 22.7 1.0
CB B:CYS100 3.7 22.4 1.0
N B:GLY98 3.8 26.1 1.0
CA B:CYS97 3.8 25.4 1.0
CA B:CYS111 3.8 12.2 1.0
N B:CYS100 3.9 26.7 1.0
N B:LEU112 4.1 15.2 1.0
N B:CYS103 4.2 17.2 1.0
C B:CYS97 4.2 27.5 1.0
CA B:CYS103 4.3 16.1 1.0
CA B:CYS100 4.4 24.4 1.0
C B:GLN96 4.4 20.6 1.0
C B:CYS111 4.4 14.2 1.0
N B:LYS99 4.5 26.1 1.0
CA B:GLN96 4.7 17.2 1.0
CA B:GLY98 4.8 26.0 1.0
O B:CYS100 4.8 22.6 1.0
N B:LYS113 4.9 22.4 1.0
C B:CYS100 4.9 23.2 1.0
O B:HOH458 4.9 34.8 1.0

Reference:

B.J.Bahnson, T.D.Colby, J.K.Chin, B.M.Goldstein, J.P.Klinman. A Link Between Protein Structure and Enzyme Catalyzed Hydrogen Tunneling. Proc.Natl.Acad.Sci.Usa V. 94 12797 1997.
ISSN: ISSN 0027-8424
PubMed: 9371755
DOI: 10.1073/PNAS.94.24.12797
Page generated: Wed Dec 16 02:45:07 2020

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