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Zinc in PDB 3ftn: Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh

Enzymatic activity of Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh

All present enzymatic activity of Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh:
1.1.1.2;

Protein crystallography data

The structure of Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh, PDB code: 3ftn was solved by F.Frolow, 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) 39.18 / 2.19
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 79.376, 83.003, 119.691, 90.00, 99.93, 90.00
R / Rfree (%) 16.5 / 22.8

Other elements in 3ftn:

The structure of Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh also contains other interesting chemical elements:

Chlorine (Cl) 6 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh (pdb code 3ftn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh, PDB code: 3ftn:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3ftn

Go back to Zinc Binding Sites List in 3ftn
Zinc binding site 1 out of 4 in the Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn354

b:36.6
occ:1.00
 OD2 A:ASP150 2.0 30.8 1.0
NE2 A:HIS59 2.1 27.8 1.0
OXT A:ACT353 2.3 27.2 1.0
SG A:CYS37 2.4 36.2 1.0
CD2 A:HIS59 3.1 33.2 1.0
CG A:ASP150 3.1 32.8 1.0
CE1 A:HIS59 3.1 27.5 1.0
CB A:CYS37 3.2 37.7 1.0
OG A:SER39 3.3 44.7 1.0
C A:ACT353 3.3 33.9 1.0
OD1 A:ASP150 3.5 36.6 1.0
O A:HOH393 3.6 47.7 0.9
CH3 A:ACT353 3.7 35.8 1.0
CB A:SER39 4.0 34.1 1.0
ND1 A:HIS59 4.2 31.3 1.0
CG A:HIS59 4.2 34.2 1.0
O A:ACT353 4.4 39.7 1.0
CB A:ASP150 4.4 24.4 1.0
OE2 A:GLU60 4.5 37.0 1.0
CE A:MET151 4.5 18.1 1.0
CA A:CYS37 4.7 31.5 1.0
CD A:GLU60 4.8 34.3 1.0

Zinc binding site 2 out of 4 in 3ftn

Go back to Zinc Binding Sites List in 3ftn
Zinc binding site 2 out of 4 in the Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn355

b:36.4
occ:1.00
 OD2 B:ASP150 1.9 30.2 1.0
NE2 B:HIS59 2.2 28.2 1.0
SG B:CYS37 2.3 34.0 1.0
OXT B:ACT353 2.5 41.7 1.0
CG B:ASP150 3.1 32.0 1.0
CB B:CYS37 3.1 29.4 1.0
CE1 B:HIS59 3.2 26.7 1.0
CD2 B:HIS59 3.2 28.0 1.0
C B:ACT353 3.3 40.8 1.0
CH3 B:ACT353 3.3 39.2 1.0
O B:HOH480 3.4 38.3 0.9
OG B:SER39 3.4 45.0 1.0
OD1 B:ASP150 3.6 35.8 1.0
CB B:SER39 4.2 43.5 1.0
ND1 B:HIS59 4.3 37.2 1.0
CB B:ASP150 4.3 27.8 1.0
CG B:HIS59 4.3 31.8 1.0
OE2 B:GLU60 4.4 38.9 1.0
O B:ACT353 4.5 37.4 1.0
CA B:CYS37 4.5 32.5 1.0
CE B:MET151 4.6 24.8 1.0
CD B:GLU60 4.7 39.2 1.0

Zinc binding site 3 out of 4 in 3ftn

Go back to Zinc Binding Sites List in 3ftn
Zinc binding site 3 out of 4 in the Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn353

b:38.3
occ:1.00
 OD2 C:ASP150 2.0 30.7 1.0
NE2 C:HIS59 2.1 33.1 1.0
SG C:CYS37 2.4 37.0 1.0
O C:ACT355 2.6 40.8 1.0
CD2 C:HIS59 3.0 38.4 1.0
CG C:ASP150 3.0 33.9 1.0
CB C:CYS37 3.1 28.1 1.0
CE1 C:HIS59 3.1 33.6 1.0
OG C:SER39 3.2 44.0 1.0
OXT C:ACT355 3.2 42.7 1.0
C C:ACT355 3.4 46.3 1.0
OD1 C:ASP150 3.4 29.0 1.0
O C:HOH451 3.5 37.5 1.0
CB C:SER39 4.1 40.2 1.0
CG C:HIS59 4.2 35.3 1.0
ND1 C:HIS59 4.2 39.6 1.0
CB C:ASP150 4.4 31.1 1.0
OE2 C:GLU60 4.4 41.9 1.0
CA C:CYS37 4.6 33.7 1.0
CE C:MET151 4.6 37.8 1.0
CD C:GLU60 4.7 35.3 1.0
CH3 C:ACT355 4.8 47.1 1.0
N C:SER39 4.9 38.1 1.0
O C:HOH463 4.9 60.0 1.0

Zinc binding site 4 out of 4 in 3ftn

Go back to Zinc Binding Sites List in 3ftn
Zinc binding site 4 out of 4 in the Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Q165E/S254K Double Mutant Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn357

b:44.8
occ:1.00
 OD2 D:ASP150 2.1 43.9 1.0
NE2 D:HIS59 2.2 45.1 1.0
O D:HOH395 2.3 47.1 1.0
SG D:CYS37 2.3 46.9 1.0
CB D:CYS37 3.0 47.0 1.0
CG D:ASP150 3.1 42.2 1.0
CE1 D:HIS59 3.2 38.5 1.0
CD2 D:HIS59 3.2 37.8 1.0
OG D:SER39 3.3 46.1 1.0
OD1 D:ASP150 3.4 37.3 1.0
O D:HOH354 4.1 52.2 1.0
CB D:SER39 4.3 49.5 1.0
ND1 D:HIS59 4.3 42.0 1.0
CG D:HIS59 4.4 41.9 1.0
CB D:ASP150 4.4 34.1 1.0
CA D:CYS37 4.5 45.4 1.0
OE2 D:GLU60 4.6 53.5 1.0
CE D:MET151 4.6 38.4 1.0
CD D:GLU60 4.7 50.0 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 13:23:41 2024

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