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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

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