error » Zinc » PDB 1d5j-1dmy » 1e3e
error »
  Zinc »
    PDB 1d5j-1dmy »
      1e3e »

Zinc in PDB 1e3e: Mouse Class II Alcohol Dehydrogenase Complex with Nadh

Enzymatic activity of Mouse Class II Alcohol Dehydrogenase Complex with Nadh

All present enzymatic activity of Mouse Class II Alcohol Dehydrogenase Complex with Nadh:
1.1.1.1;

Protein crystallography data

The structure of Mouse Class II Alcohol Dehydrogenase Complex with Nadh, PDB code: 1e3e was solved by S.Svensson, J.O.Hoeoeg, G.Schneider, T.Sandalova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.12
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 81.275, 82.900, 105.528, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 25.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh (pdb code 1e3e). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh, PDB code: 1e3e:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1e3e

Go back to Zinc Binding Sites List in 1e3e
Zinc binding site 1 out of 4 in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mouse Class II Alcohol Dehydrogenase Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn378

b:27.0
occ:1.00
NE2 A:HIS67 2.1 21.1 1.0
O A:HOH2222 2.1 19.5 1.0
SG A:CYS178 2.4 23.4 1.0
SG A:CYS46 2.6 28.9 1.0
CE1 A:HIS67 3.0 24.6 1.0
CD2 A:HIS67 3.1 23.8 1.0
CB A:CYS46 3.5 29.6 1.0
CB A:CYS178 3.6 19.7 1.0
OG1 A:THR48 3.7 32.1 1.0
ND1 A:HIS67 4.1 23.4 1.0
CB A:THR48 4.1 31.2 1.0
O A:HOH2220 4.2 20.9 1.0
O A:HOH2115 4.2 42.2 1.0
CG A:HIS67 4.2 24.3 1.0
C5N A:NAI377 4.2 27.9 1.0
C6N A:NAI377 4.5 29.4 1.0
OE1 A:GLU68 4.8 26.0 1.0

Zinc binding site 2 out of 4 in 1e3e

Go back to Zinc Binding Sites List in 1e3e
Zinc binding site 2 out of 4 in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Mouse Class II Alcohol Dehydrogenase Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn379

b:24.6
occ:1.00
SG A:CYS103 2.3 19.6 1.0
SG A:CYS111 2.4 16.8 1.0
SG A:CYS97 2.4 23.3 1.0
SG A:CYS100 2.5 23.0 1.0
CB A:CYS97 3.4 18.5 1.0
CB A:CYS111 3.4 20.9 1.0
CB A:CYS103 3.4 21.0 1.0
N A:CYS97 3.5 19.9 1.0
CB A:CYS100 3.6 22.1 1.0
N A:GLY112 3.8 24.9 1.0
CA A:CYS97 3.9 20.5 1.0
CA A:CYS111 3.9 21.2 1.0
N A:LYS98 3.9 19.4 1.0
O A:HOH2087 4.1 21.3 1.0
N A:CYS100 4.1 22.8 1.0
C A:CYS97 4.3 21.3 1.0
C A:CYS111 4.3 24.4 1.0
N A:ARG99 4.3 21.3 1.0
N A:CYS103 4.4 19.6 1.0
CA A:CYS100 4.4 23.8 1.0
CA A:CYS103 4.5 20.4 1.0
C A:GLN96 4.6 21.8 1.0
C A:ARG99 4.7 23.0 1.0
CA A:GLY112 4.8 27.2 1.0
CA A:LYS98 4.8 20.7 1.0
CA A:GLN96 4.9 20.8 1.0
N A:LYS113 4.9 31.7 1.0
C A:LYS98 5.0 20.4 1.0

Zinc binding site 3 out of 4 in 1e3e

Go back to Zinc Binding Sites List in 1e3e
Zinc binding site 3 out of 4 in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Mouse Class II Alcohol Dehydrogenase Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn378

b:26.2
occ:1.00
NE2 B:HIS67 2.3 22.5 1.0
SG B:CYS178 2.4 24.2 1.0
SG B:CYS46 2.5 24.7 1.0
O B:HOH2280 2.6 27.0 1.0
CE1 B:HIS67 3.2 23.6 1.0
CD2 B:HIS67 3.3 22.9 1.0
CB B:CYS46 3.5 23.1 1.0
CB B:CYS178 3.7 21.1 1.0
O B:HOH2268 3.9 20.4 1.0
OG1 B:THR48 4.1 28.4 1.0
C5N B:NAI377 4.2 21.4 1.0
ND1 B:HIS67 4.3 23.7 1.0
CG B:HIS67 4.4 22.9 1.0
CB B:THR48 4.4 29.5 1.0
C6N B:NAI377 4.5 21.9 1.0
OE1 B:GLU68 4.9 20.8 1.0
CA B:CYS46 5.0 24.4 1.0

Zinc binding site 4 out of 4 in 1e3e

Go back to Zinc Binding Sites List in 1e3e
Zinc binding site 4 out of 4 in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Mouse Class II Alcohol Dehydrogenase Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn379

b:43.1
occ:1.00
SG B:CYS103 2.1 36.3 1.0
SG B:CYS111 2.3 34.3 1.0
SG B:CYS97 2.5 40.8 1.0
SG B:CYS100 2.6 44.7 1.0
N B:CYS97 3.4 35.8 1.0
CB B:CYS100 3.5 43.9 1.0
CB B:CYS97 3.5 38.4 1.0
CB B:CYS103 3.5 43.1 1.0
CB B:CYS111 3.5 34.5 1.0
N B:LYS98 3.6 40.0 1.0
CA B:CYS97 3.8 38.2 1.0
N B:GLY112 3.8 35.7 1.0
CA B:CYS111 4.1 34.9 1.0
C B:CYS97 4.1 39.1 1.0
N B:CYS100 4.1 44.4 1.0
C B:GLN96 4.3 33.8 1.0
N B:CYS103 4.3 43.6 1.0
CA B:CYS100 4.3 43.6 1.0
N B:ARG99 4.3 45.7 1.0
C B:CYS111 4.4 35.8 1.0
CA B:CYS103 4.5 42.4 1.0
CA B:LYS98 4.6 43.0 1.0
CA B:GLN96 4.6 30.9 1.0
N B:LYS113 4.7 38.4 1.0
CA B:GLY112 4.8 36.8 1.0
C B:CYS100 4.9 43.5 1.0
O B:CYS100 4.9 41.0 1.0
C B:ARG99 5.0 44.6 1.0

Reference:

S.Svensson, J.O.Hoeoeg, G.Schneider, T.Sandalova. Crystal Structure of Mouse Class II Alcohol Dehydrogenase Reveal Determinants of Substrate Specificity and Catalytic Efficiency J.Mol.Biol. V. 302 441 2000.
ISSN: ISSN 0022-2836
PubMed: 10970744
DOI: 10.1006/JMBI.2000.4039
Page generated: Fri Sep 25 21:22:08 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy