Atomistry » Zinc » PDB 3hqz-3i4n » 3hud
Atomistry »
  Zinc »
    PDB 3hqz-3i4n »
      3hud »

Zinc in PDB 3hud: The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions

Enzymatic activity of The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions

All present enzymatic activity of The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions:
1.1.1.1;

Protein crystallography data

The structure of The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions, PDB code: 3hud was solved by T.D.Hurley, W.F.Bosron, J.A.Hamilton, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 3.20
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 54.590, 45.050, 93.860, 91.93, 102.50, 68.82
R / Rfree (%) 17.9 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions (pdb code 3hud). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions, PDB code: 3hud:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3hud

Go back to Zinc Binding Sites List in 3hud
Zinc binding site 1 out of 4 in the The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn375

b:25.0
occ:1.00
 SG A:CYS97 2.2 25.0 1.0
SG A:CYS103 2.3 25.0 1.0
SG A:CYS111 2.3 25.0 1.0
SG A:CYS100 2.3 25.0 1.0
CB A:CYS97 3.0 25.0 1.0
CB A:CYS111 3.1 25.0 1.0
CB A:CYS103 3.2 25.0 1.0
CB A:CYS100 3.3 25.0 1.0
N A:CYS97 3.5 25.0 1.0
CA A:CYS97 3.7 25.0 1.0
CA A:CYS111 3.8 25.0 1.0
N A:CYS100 3.9 25.0 1.0
N A:GLY98 4.0 25.0 1.0
N A:LEU112 4.1 25.0 1.0
CA A:CYS100 4.2 25.0 1.0
C A:CYS97 4.3 25.0 1.0
CA A:CYS103 4.3 25.0 1.0
N A:CYS103 4.3 25.0 1.0
C A:CYS111 4.4 25.0 1.0
C A:GLN96 4.4 25.0 1.0
NZ A:LYS113 4.6 25.0 1.0
N A:LYS99 4.7 25.0 1.0
O A:CYS100 4.8 25.0 1.0
CA A:GLN96 4.8 25.0 1.0
C A:CYS100 4.9 25.0 1.0
CG A:LYS113 4.9 25.0 1.0

Zinc binding site 2 out of 4 in 3hud

Go back to Zinc Binding Sites List in 3hud
Zinc binding site 2 out of 4 in the The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn376

b:25.0
occ:1.00
 SG A:CYS174 2.1 25.0 1.0
NE2 A:HIS67 2.2 25.0 1.0
SG A:CYS46 2.5 25.0 1.0
CE1 A:HIS67 2.7 25.0 1.0
CD2 A:HIS67 3.1 25.0 1.0
CB A:CYS174 3.1 25.0 1.0
CB A:CYS46 3.2 25.0 1.0
C5N A:NAD377 3.6 25.0 1.0
ND1 A:HIS67 3.6 25.0 1.0
CG A:HIS67 3.8 25.0 1.0
OG1 A:THR48 4.0 25.0 1.0
CB A:THR48 4.2 25.0 1.0
C6N A:NAD377 4.4 25.0 1.0
C4N A:NAD377 4.4 25.0 1.0
OE2 A:GLU68 4.5 25.0 1.0
CA A:CYS174 4.7 25.0 1.0
CA A:CYS46 4.7 25.0 1.0
CE2 A:PHE93 5.0 25.0 1.0

Zinc binding site 3 out of 4 in 3hud

Go back to Zinc Binding Sites List in 3hud
Zinc binding site 3 out of 4 in the The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn375

b:25.0
occ:1.00
 SG B:CYS100 2.2 25.0 1.0
SG B:CYS103 2.2 25.0 1.0
SG B:CYS97 2.3 25.0 1.0
SG B:CYS111 2.3 25.0 1.0
CB B:CYS100 3.1 25.0 1.0
CB B:CYS103 3.2 25.0 1.0
CB B:CYS97 3.2 25.0 1.0
CB B:CYS111 3.2 25.0 1.0
N B:CYS97 3.5 25.0 1.0
CA B:CYS111 3.7 25.0 1.0
N B:CYS100 3.8 25.0 1.0
CA B:CYS97 3.8 25.0 1.0
N B:GLY98 4.0 25.0 1.0
CA B:CYS100 4.0 25.0 1.0
N B:LEU112 4.0 25.0 1.0
N B:CYS103 4.2 25.0 1.0
CA B:CYS103 4.2 25.0 1.0
C B:CYS97 4.3 25.0 1.0
C B:CYS111 4.4 25.0 1.0
C B:GLN96 4.5 25.0 1.0
O B:CYS100 4.6 25.0 1.0
C B:CYS100 4.6 25.0 1.0
CA B:GLN96 4.9 25.0 1.0
C B:GLY98 4.9 25.0 1.0
N B:LYS99 4.9 25.0 1.0
C B:LYS99 4.9 25.0 1.0
N B:CYS111 4.9 25.0 1.0
CB B:LEU112 4.9 25.0 1.0

Zinc binding site 4 out of 4 in 3hud

Go back to Zinc Binding Sites List in 3hud
Zinc binding site 4 out of 4 in the The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of The Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn376

b:25.0
occ:1.00
 NE2 B:HIS67 2.1 25.0 1.0
SG B:CYS174 2.3 25.0 1.0
SG B:CYS46 2.4 25.0 1.0
CD2 B:HIS67 3.1 25.0 1.0
CE1 B:HIS67 3.1 25.0 1.0
C5N B:NAD377 3.3 25.0 1.0
CB B:CYS46 3.3 25.0 1.0
CB B:CYS174 3.4 25.0 1.0
OG1 B:THR48 4.0 25.0 1.0
CB B:THR48 4.0 25.0 1.0
C6N B:NAD377 4.0 25.0 1.0
C4N B:NAD377 4.1 25.0 1.0
OE1 B:GLU68 4.1 25.0 1.0
ND1 B:HIS67 4.2 25.0 1.0
CG B:HIS67 4.2 25.0 1.0
N B:THR48 4.7 25.0 1.0
CA B:CYS46 4.8 25.0 1.0
CA B:CYS174 4.9 25.0 1.0
CA B:THR48 4.9 25.0 1.0

Reference:

T.D.Hurley, W.F.Bosron, J.A.Hamilton, L.M.Amzel. Structure of Human Beta 1 Beta 1 Alcohol Dehydrogenase: Catalytic Effects of Non-Active-Site Substitutions. Proc.Natl.Acad.Sci.Usa V. 88 8149 1991.
ISSN: ISSN 0027-8424
PubMed: 1896463
DOI: 10.1073/PNAS.88.18.8149
Page generated: Sat Oct 26 06:42:32 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