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Arsenic 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:

Zinc (Zn) 4 atoms
Sodium (Na) 2 atoms

Arsenic Binding Sites:

The binding sites of Arsenic 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 Arsenic atom.
In total 4 binding sites of Arsenic 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 Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in 3fpc

Go back to Arsenic Binding Sites List in 3fpc
Arsenic 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 Arsenic with other atoms in the As 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:As354

b:11.4
occ:1.00
 AS A:CAC354 0.0 11.4 1.0
O2 A:CAC354 1.7 8.5 1.0
O1 A:CAC354 1.8 13.5 1.0
C1 A:CAC354 1.9 10.7 1.0
C2 A:CAC354 1.9 12.8 1.0
ZN A:ZN353 3.3 7.8 1.0
OD1 A:ASP150 3.6 11.5 1.0
O A:HOH366 3.7 9.1 1.0
O A:HOH2038 3.7 50.3 1.0
OD2 A:ASP150 3.7 8.8 1.0
OG A:SER39 3.8 9.0 1.0
CG A:ASP150 4.0 7.8 1.0
O A:HOH464 4.0 36.1 1.0
NE2 A:HIS59 4.2 6.9 1.0
CB A:SER39 4.5 7.8 1.0
CD1 A:LEU294 4.7 7.8 1.0
OG1 A:THR154 4.7 7.3 1.0
CD2 A:HIS59 4.7 6.6 1.0
CE2 A:TRP110 4.8 11.6 1.0
CZ2 A:TRP110 4.8 14.1 1.0
CE1 A:HIS59 4.8 9.1 1.0
SG A:CYS295 5.0 8.0 1.0
CD2 A:TRP110 5.0 9.2 1.0

Arsenic binding site 2 out of 4 in 3fpc

Go back to Arsenic Binding Sites List in 3fpc
Arsenic 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 Arsenic with other atoms in the As 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:As354

b:11.8
occ:1.00
 AS B:CAC354 0.0 11.8 1.0
O1 B:CAC354 1.7 8.8 1.0
O2 B:CAC354 1.7 12.3 1.0
C2 B:CAC354 1.9 12.4 1.0
C1 B:CAC354 1.9 10.9 1.0
ZN B:ZN353 3.3 8.1 1.0
OD1 B:ASP150 3.6 10.7 1.0
O B:HOH371 3.7 9.6 1.0
OG B:SER39 3.8 9.9 1.0
OD2 B:ASP150 3.8 9.0 1.0
CG B:ASP150 4.0 7.2 1.0
NE2 B:HIS59 4.2 6.5 1.0
O B:HOH483 4.2 33.2 1.0
CB B:SER39 4.5 8.4 1.0
CD1 B:LEU294 4.7 6.8 1.0
CE2 B:TRP110 4.7 9.6 1.0
OG1 B:THR154 4.7 7.1 1.0
CZ2 B:TRP110 4.7 13.0 1.0
CD2 B:HIS59 4.7 7.1 1.0
CE1 B:HIS59 4.8 7.8 1.0
CH2 B:TRP110 4.9 12.6 1.0
CD2 B:TRP110 4.9 9.5 1.0
SG B:CYS295 5.0 8.4 1.0

Arsenic binding site 3 out of 4 in 3fpc

Go back to Arsenic Binding Sites List in 3fpc
Arsenic 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 Arsenic with other atoms in the As 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:As354

b:10.3
occ:1.00
 AS C:CAC354 0.0 10.3 1.0
O2 C:CAC354 1.7 6.5 1.0
O1 C:CAC354 1.8 14.3 1.0
C2 C:CAC354 1.9 9.3 1.0
C1 C:CAC354 1.9 9.0 1.0
ZN C:ZN353 3.3 6.6 1.0
OD1 C:ASP150 3.6 10.0 1.0
O C:HOH372 3.6 8.2 1.0
OD2 C:ASP150 3.8 7.7 1.0
OG C:SER39 3.8 7.5 1.0
O2 C:EDO357 4.0 29.5 0.5
CG C:ASP150 4.0 6.4 1.0
NE2 C:HIS59 4.1 6.5 1.0
C1 C:EDO357 4.3 14.6 0.5
CB C:SER39 4.5 7.8 1.0
C2 C:EDO357 4.5 26.4 0.5
CD1 C:LEU294 4.7 8.3 1.0
CD2 C:HIS59 4.7 7.3 1.0
OG1 C:THR154 4.7 5.9 1.0
CE2 C:TRP110 4.7 9.7 1.0
CZ2 C:TRP110 4.7 11.0 1.0
CE1 C:HIS59 4.8 8.0 1.0
CD2 C:TRP110 4.9 6.8 1.0
C1 C:EDO357 4.9 22.1 0.5
SG C:CYS295 5.0 7.8 1.0
CH2 C:TRP110 5.0 11.5 1.0
SG C:CYS37 5.0 7.1 1.0

Arsenic binding site 4 out of 4 in 3fpc

Go back to Arsenic Binding Sites List in 3fpc
Arsenic 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 Arsenic with other atoms in the As 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:As354

b:12.2
occ:1.00
 AS D:CAC354 0.0 12.2 1.0
O2 D:CAC354 1.7 8.5 1.0
O1 D:CAC354 1.8 13.7 1.0
C1 D:CAC354 1.9 11.4 1.0
C2 D:CAC354 1.9 11.9 1.0
ZN D:ZN353 3.3 7.9 1.0
OD1 D:ASP150 3.5 11.4 1.0
O D:HOH377 3.7 8.7 1.0
OD2 D:ASP150 3.7 10.3 1.0
OG D:SER39 3.8 9.2 1.0
CG D:ASP150 4.0 8.2 1.0
NE2 D:HIS59 4.2 7.9 1.0
CB D:SER39 4.5 8.9 1.0
CD1 D:LEU294 4.6 9.3 1.0
OG1 D:THR154 4.7 7.0 1.0
CD2 D:HIS59 4.7 6.2 1.0
C1 D:EDO360 4.7 22.6 0.5
CE2 D:TRP110 4.7 9.5 1.0
CZ2 D:TRP110 4.7 12.9 1.0
CE1 D:HIS59 4.8 10.5 1.0
O2 D:EDO360 4.9 19.7 0.5
SG D:CYS295 5.0 9.1 1.0
CH2 D:TRP110 5.0 13.5 1.0
CD2 D:TRP110 5.0 7.9 1.0
C2 D:EDO360 5.0 20.8 0.5

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: Wed Jul 10 11:40:08 2024

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