Atomistry » Zinc » PDB 1jpu-1k53 » 1ju9
Atomistry »
  Zinc »
    PDB 1jpu-1k53 »
      1ju9 »

Zinc in PDB 1ju9: Horse Liver Alcohol Dehydrogenase VAL292SER Mutant

Enzymatic activity of Horse Liver Alcohol Dehydrogenase VAL292SER Mutant

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase VAL292SER Mutant:
1.1.1.1;

Protein crystallography data

The structure of Horse Liver Alcohol Dehydrogenase VAL292SER Mutant, PDB code: 1ju9 was solved by J.K.Rubach, 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 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 46.271, 180.398, 46.176, 90.00, 106.65, 90.00
R / Rfree (%) 19.6 / 23.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase VAL292SER Mutant (pdb code 1ju9). 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 VAL292SER Mutant, PDB code: 1ju9:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1ju9

Go back to Zinc Binding Sites List in 1ju9
Zinc binding site 1 out of 4 in the Horse Liver Alcohol Dehydrogenase VAL292SER Mutant


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 VAL292SER Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn375

b:29.9
occ:1.00
NE2 A:HIS67 2.1 21.4 1.0
O A:HOH437 2.2 21.4 1.0
SG A:CYS174 2.3 23.1 1.0
SG A:CYS46 2.4 25.1 1.0
CD2 A:HIS67 3.0 21.0 1.0
CE1 A:HIS67 3.1 22.1 1.0
CB A:CYS46 3.3 23.3 1.0
CB A:CYS174 3.4 22.0 1.0
OG A:SER48 4.0 24.3 1.0
CB A:SER48 4.1 23.2 1.0
ND1 A:HIS67 4.2 21.2 1.0
CG A:HIS67 4.2 20.5 1.0
CA A:CYS46 4.8 23.5 1.0
CA A:CYS174 4.8 22.7 1.0
N A:SER48 4.9 23.7 1.0

Zinc binding site 2 out of 4 in 1ju9

Go back to Zinc Binding Sites List in 1ju9
Zinc binding site 2 out of 4 in the Horse Liver Alcohol Dehydrogenase VAL292SER Mutant


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 VAL292SER Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn376

b:25.7
occ:1.00
SG A:CYS103 2.2 22.3 1.0
SG A:CYS100 2.2 28.1 1.0
SG A:CYS111 2.4 24.6 1.0
SG A:CYS97 2.4 26.2 1.0
CB A:CYS111 3.2 22.3 1.0
CB A:CYS103 3.3 24.4 1.0
CB A:CYS97 3.4 25.7 1.0
CB A:CYS100 3.5 28.7 1.0
N A:CYS97 3.6 25.1 1.0
CA A:CYS111 3.7 22.9 1.0
N A:CYS100 3.8 29.8 1.0
N A:GLY98 3.9 27.5 1.0
CA A:CYS97 3.9 25.8 1.0
N A:LEU112 4.0 23.8 1.0
N A:CYS103 4.1 23.9 1.0
CA A:CYS100 4.2 28.7 1.0
C A:CYS111 4.2 23.5 1.0
CA A:CYS103 4.3 24.3 1.0
C A:CYS97 4.3 27.0 1.0
N A:LYS99 4.5 30.7 1.0
C A:GLN96 4.7 24.0 1.0
N A:LYS113 4.7 25.7 1.0
CG A:LYS113 4.8 28.4 1.0
O A:CYS100 4.9 26.6 1.0
C A:CYS100 4.9 27.9 1.0
CA A:GLY98 4.9 29.1 1.0
CA A:GLN96 5.0 23.2 1.0
C A:LYS99 5.0 31.4 1.0

Zinc binding site 3 out of 4 in 1ju9

Go back to Zinc Binding Sites List in 1ju9
Zinc binding site 3 out of 4 in the Horse Liver Alcohol Dehydrogenase VAL292SER Mutant


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 VAL292SER Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn375

b:30.3
occ:1.00
NE2 B:HIS67 2.0 20.8 1.0
O B:HOH433 2.1 20.5 1.0
SG B:CYS174 2.4 22.4 1.0
SG B:CYS46 2.4 25.6 1.0
CE1 B:HIS67 3.0 21.5 1.0
CD2 B:HIS67 3.0 20.7 1.0
CB B:CYS46 3.4 24.0 1.0
CB B:CYS174 3.4 22.2 1.0
CB B:SER48 4.1 24.6 1.0
OG B:SER48 4.1 26.0 1.0
ND1 B:HIS67 4.1 20.5 1.0
CG B:HIS67 4.2 21.4 1.0
CA B:CYS174 4.8 22.3 1.0
CA B:CYS46 4.9 23.8 1.0
N B:SER48 4.9 24.8 1.0
CE2 B:PHE93 4.9 18.6 1.0

Zinc binding site 4 out of 4 in 1ju9

Go back to Zinc Binding Sites List in 1ju9
Zinc binding site 4 out of 4 in the Horse Liver Alcohol Dehydrogenase VAL292SER Mutant


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 VAL292SER Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn376

b:25.6
occ:1.00
SG B:CYS103 2.2 22.8 1.0
SG B:CYS100 2.3 25.6 1.0
SG B:CYS97 2.4 26.8 1.0
SG B:CYS111 2.4 23.2 1.0
CB B:CYS111 3.2 21.8 1.0
CB B:CYS103 3.3 24.2 1.0
CB B:CYS100 3.4 27.1 1.0
CB B:CYS97 3.4 26.0 1.0
N B:CYS97 3.6 25.1 1.0
CA B:CYS111 3.7 22.9 1.0
N B:GLY98 3.8 27.8 1.0
N B:CYS100 3.9 29.0 1.0
CA B:CYS97 4.0 26.0 1.0
N B:LEU112 4.0 23.8 1.0
N B:CYS103 4.1 24.3 1.0
CA B:CYS100 4.2 26.9 1.0
C B:CYS111 4.2 23.3 1.0
CA B:CYS103 4.3 24.4 1.0
C B:CYS97 4.3 27.0 1.0
N B:LYS99 4.4 30.9 1.0
C B:GLN96 4.6 24.1 1.0
O B:CYS100 4.8 24.8 1.0
C B:CYS100 4.8 26.1 1.0
CA B:GLY98 4.8 29.9 1.0
CG B:LYS113 4.8 26.8 1.0
N B:LYS113 4.9 24.4 1.0
CA B:GLN96 4.9 24.1 1.0
N B:CYS111 5.0 21.5 1.0

Reference:

J.K.Rubach, S.Ramaswamy, B.V.Plapp. Contributions of Valine-292 in the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase and Dynamics to Catalysis. Biochemistry V. 40 12686 2001.
ISSN: ISSN 0006-2960
PubMed: 11601993
DOI: 10.1021/BI011540R
Page generated: Sun Oct 13 03:51:42 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy