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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: Wed Dec 16 04:25:04 2020

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