Atomistry » Zinc » PDB 3fki-3fui » 3fpc
Atomistry »
  Zinc »
    PDB 3fki-3fui »
      3fpc »

Zinc in PDB 3fpc: Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh

Enzymatic activity of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh

All present enzymatic activity of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh:
1.1.1.2;

Protein crystallography data

The structure of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh, PDB code: 3fpc was solved by F.Felix, E.Goihberg, L.Shimon, Y.Burstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.77 / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 79.742, 82.429, 118.249, 90.00, 99.89, 90.00
R / Rfree (%) 11.6 / 15.5

Other elements in 3fpc:

The structure of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh also contains other interesting chemical elements:

Arsenic (As) 4 atoms
Sodium (Na) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh (pdb code 3fpc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh, PDB code: 3fpc:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3fpc

Go back to Zinc Binding Sites List in 3fpc
Zinc binding site 1 out of 4 in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn353

b:7.8
occ:1.00
 O2 A:CAC354 1.9 8.5 1.0
OD2 A:ASP150 2.0 8.8 1.0
NE2 A:HIS59 2.0 6.9 1.0
SG A:CYS37 2.3 7.9 1.0
CE1 A:HIS59 3.0 9.1 1.0
CD2 A:HIS59 3.0 6.6 1.0
CG A:ASP150 3.1 7.8 1.0
CB A:CYS37 3.1 7.9 1.0
AS A:CAC354 3.3 11.4 1.0
O A:HOH2038 3.4 50.3 1.0
OD1 A:ASP150 3.6 11.5 1.0
OG A:SER39 3.7 9.0 1.0
C2 A:CAC354 3.9 12.8 1.0
O1 A:CAC354 3.9 13.5 1.0
CB A:SER39 3.9 7.8 1.0
ND1 A:HIS59 4.1 8.3 1.0
OE2 A:GLU60 4.2 11.5 1.0
CG A:HIS59 4.2 6.8 1.0
CB A:ASP150 4.3 6.6 1.0
CE A:MET151 4.3 11.9 1.0
CD A:GLU60 4.5 10.2 1.0
CA A:CYS37 4.6 6.2 1.0
C1 A:CAC354 4.8 10.7 1.0
N A:SER39 4.8 6.5 1.0
CG A:GLU60 4.9 7.2 1.0
OE1 A:GLU60 5.0 9.9 1.0
O A:HOH370 5.0 8.2 1.0

Zinc binding site 2 out of 4 in 3fpc

Go back to Zinc Binding Sites List in 3fpc
Zinc binding site 2 out of 4 in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn353

b:8.1
occ:1.00
 O1 B:CAC354 2.0 8.8 1.0
OD2 B:ASP150 2.0 9.0 1.0
NE2 B:HIS59 2.0 6.5 1.0
SG B:CYS37 2.3 8.4 1.0
CD2 B:HIS59 3.0 7.1 1.0
CE1 B:HIS59 3.0 7.8 1.0
CG B:ASP150 3.1 7.2 1.0
CB B:CYS37 3.2 9.4 1.0
AS B:CAC354 3.3 11.8 1.0
OD1 B:ASP150 3.6 10.7 1.0
OG B:SER39 3.7 9.9 1.0
O2 B:CAC354 3.9 12.3 1.0
C1 B:CAC354 3.9 10.9 1.0
CB B:SER39 3.9 8.4 1.0
ND1 B:HIS59 4.1 9.7 1.0
CG B:HIS59 4.1 6.4 1.0
OE2 B:GLU60 4.2 11.6 1.0
CB B:ASP150 4.3 8.1 1.0
CE B:MET151 4.3 9.9 1.0
CD B:GLU60 4.6 12.2 1.0
CA B:CYS37 4.6 8.1 1.0
N B:SER39 4.8 7.8 1.0
C2 B:CAC354 4.9 12.4 1.0
CG B:GLU60 4.9 9.4 1.0

Zinc binding site 3 out of 4 in 3fpc

Go back to Zinc Binding Sites List in 3fpc
Zinc binding site 3 out of 4 in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn353

b:6.6
occ:1.00
 O2 C:CAC354 2.0 6.5 1.0
OD2 C:ASP150 2.0 7.7 1.0
NE2 C:HIS59 2.0 6.5 1.0
SG C:CYS37 2.3 7.1 1.0
CD2 C:HIS59 3.0 7.3 1.0
CE1 C:HIS59 3.0 8.0 1.0
CG C:ASP150 3.1 6.4 1.0
CB C:CYS37 3.1 8.2 1.0
AS C:CAC354 3.3 10.3 1.0
OD1 C:ASP150 3.5 10.0 1.0
OG C:SER39 3.7 7.5 1.0
O1 C:CAC354 3.9 14.3 1.0
CB C:SER39 3.9 7.8 1.0
C2 C:CAC354 3.9 9.3 1.0
OE2 C:GLU60 4.1 10.8 1.0
ND1 C:HIS59 4.1 8.6 1.0
CG C:HIS59 4.1 6.8 1.0
O2 C:EDO357 4.2 29.5 0.5
CB C:ASP150 4.3 6.0 1.0
CE C:MET151 4.3 8.0 1.0
CD C:GLU60 4.5 10.3 1.0
CA C:CYS37 4.6 6.5 1.0
C1 C:CAC354 4.9 9.0 1.0
N C:SER39 4.9 6.9 1.0
C2 C:EDO357 4.9 13.7 0.5
CG C:GLU60 5.0 7.4 1.0

Zinc binding site 4 out of 4 in 3fpc

Go back to Zinc Binding Sites List in 3fpc
Zinc binding site 4 out of 4 in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-294 of T. Brockii Adh By E. Histolytica Adh within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn353

b:7.9
occ:1.00
 O2 D:CAC354 1.9 8.5 1.0
OD2 D:ASP150 1.9 10.3 1.0
NE2 D:HIS59 2.1 7.9 1.0
SG D:CYS37 2.3 8.1 1.0
CD2 D:HIS59 3.0 6.2 1.0
CG D:ASP150 3.1 8.2 1.0
CE1 D:HIS59 3.1 10.5 1.0
CB D:CYS37 3.1 8.1 1.0
AS D:CAC354 3.3 12.2 1.0
OD1 D:ASP150 3.6 11.4 1.0
OG D:SER39 3.7 9.2 1.0
C2 D:CAC354 3.9 11.9 1.0
O1 D:CAC354 3.9 13.7 1.0
CB D:SER39 3.9 8.9 1.0
ND1 D:HIS59 4.2 9.3 1.0
OE2 D:GLU60 4.2 12.8 1.0
CG D:HIS59 4.2 6.6 1.0
CB D:ASP150 4.2 8.4 1.0
CE D:MET151 4.3 9.6 1.0
C1 D:EDO360 4.5 22.6 0.5
CD D:GLU60 4.6 11.8 1.0
CA D:CYS37 4.6 8.4 1.0
C1 D:CAC354 4.8 11.4 1.0
N D:SER39 4.8 8.3 1.0
CG D:GLU60 5.0 9.3 1.0

Reference:

E.Goihberg, M.Peretz, S.Tel-Or, O.Dym, L.Shimon, F.Frolow, Y.Burstein. Biochemical and Structural Properties of Chimeras Constructed By Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases From Thermophilic and Mesophilic Microorganisms Biochemistry V. 49 1943 2010.
ISSN: ISSN 0006-2960
PubMed: 20102159
DOI: 10.1021/BI901730X
Page generated: Thu Oct 24 13:20:59 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy