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Zinc in PDB 3fsr: 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 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 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 Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh, PDB code: 3fsr was solved by F.Frolow, H.Greenblatt, E.Goihberg, Y.Burstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.42 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 79.291, 101.427, 113.169, 90.00, 94.19, 90.00
R / Rfree (%) 16.1 / 22

Zinc Binding Sites:

The binding sites of Zinc atom in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh (pdb code 3fsr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of T. Brockii Adh By C. Beijerinckii Adh, PDB code: 3fsr:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 3fsr

Go back to Zinc Binding Sites List in 3fsr
Zinc binding site 1 out of 6 in the 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 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:Zn353

b:53.6
occ:0.53
OD2 A:ASP150 2.0 37.3 1.0
NE2 A:HIS59 2.4 26.0 1.0
SG A:CYS37 2.7 39.4 1.0
CG A:ASP150 3.1 27.2 1.0
O2 A:EDO355 3.2 58.0 1.0
O A:HOH630 3.2 45.6 1.0
CD2 A:HIS59 3.3 26.4 1.0
OG A:SER39 3.3 67.3 1.0
CE1 A:HIS59 3.4 38.2 1.0
C1 A:EDO355 3.5 64.2 1.0
CB A:CYS37 3.6 28.9 1.0
OD1 A:ASP150 3.6 30.0 1.0
C2 A:EDO355 3.6 62.0 1.0
O1 A:EDO355 3.9 63.9 1.0
CB A:SER39 4.0 64.0 1.0
CB A:ASP150 4.3 15.5 1.0
CE A:MET151 4.4 20.6 1.0
ND1 A:HIS59 4.5 37.9 1.0
OE2 A:GLU60 4.5 21.9 1.0
CG A:HIS59 4.5 25.9 1.0
CD A:GLU60 4.8 31.6 1.0

Zinc binding site 2 out of 6 in 3fsr

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Zinc binding site 2 out of 6 in the 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 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:25.2
occ:0.63
O A:HIS287 2.8 16.8 1.0
OG1 A:THR289 2.8 17.6 1.0
O A:HOH382 2.8 16.3 1.0
O2 A:EDO356 2.9 15.9 0.5
C2 A:EDO356 2.9 22.8 0.5
O A:GLY259 2.9 22.1 1.0
O A:GLY260 3.0 21.7 1.0
C1 A:EDO356 3.0 20.2 0.5
OH C:TYR99 3.0 23.5 1.0
C A:GLY259 3.4 20.3 1.0
O1 A:EDO356 3.5 13.9 0.5
O2 A:EDO356 3.7 25.4 0.5
CB A:THR289 3.8 16.1 1.0
C A:GLY260 3.8 16.4 1.0
CZ C:TYR99 3.9 22.4 1.0
C A:HIS287 3.9 20.0 1.0
N A:THR289 4.0 18.1 1.0
CA A:GLY259 4.0 19.6 1.0
CG1 A:ILE261 4.1 12.8 1.0
O A:HOH358 4.1 5.2 1.0
N A:GLY260 4.1 18.6 1.0
CA A:GLY260 4.4 14.2 1.0
CB A:HIS287 4.4 13.3 1.0
C2 A:EDO356 4.4 25.7 0.5
CE1 C:TYR99 4.5 20.8 1.0
CA A:THR289 4.5 12.8 1.0
O C:HOH451 4.5 37.8 1.0
CE2 C:TYR99 4.7 17.2 1.0
CA A:HIS287 4.7 16.2 1.0
C1 A:EDO356 4.8 29.9 0.5
N A:ILE261 4.8 18.5 1.0
N A:LYS288 4.9 8.9 1.0
CD1 A:ILE261 4.9 13.5 1.0
CA A:LYS288 5.0 15.6 1.0
C A:LYS288 5.0 22.6 1.0
N A:GLY259 5.0 20.4 1.0

Zinc binding site 3 out of 6 in 3fsr

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Zinc binding site 3 out of 6 in the 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 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:Zn353

b:24.0
occ:0.59
O B:GLY259 2.7 25.3 1.0
O B:HIS287 2.8 16.8 1.0
OG1 B:THR289 2.8 20.9 1.0
O D:HOH744 2.9 51.6 1.0
O B:GLY260 3.0 19.7 1.0
OH D:TYR99 3.0 31.5 1.0
O D:HOH387 3.0 25.9 1.0
C B:GLY259 3.3 22.1 1.0
O D:HOH866 3.8 47.0 1.0
CB B:THR289 3.9 16.1 1.0
C B:GLY260 3.9 24.9 1.0
CZ D:TYR99 3.9 33.4 1.0
CG1 B:ILE261 3.9 23.4 1.0
C B:HIS287 3.9 19.4 1.0
CA B:GLY259 3.9 23.4 1.0
O B:HOH459 3.9 39.8 1.0
N B:THR289 4.0 19.5 1.0
N B:GLY260 4.1 18.6 1.0
O B:HOH356 4.2 7.8 1.0
CB B:HIS287 4.4 11.2 1.0
CA B:GLY260 4.4 19.2 1.0
CE1 D:TYR99 4.5 32.0 1.0
CA B:THR289 4.6 14.6 1.0
CD1 B:ILE261 4.6 25.9 1.0
CE2 D:TYR99 4.6 29.7 1.0
CA B:HIS287 4.7 20.4 1.0
O B:HOH538 4.8 34.2 1.0
N B:ILE261 4.8 15.6 1.0
N B:LYS288 4.9 15.4 1.0
CA B:LYS288 4.9 16.8 1.0
C B:LYS288 4.9 17.4 1.0
N B:GLY259 4.9 22.7 1.0

Zinc binding site 4 out of 6 in 3fsr

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Zinc binding site 4 out of 6 in the 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 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:53.6
occ:0.49
OD2 C:ASP150 2.0 39.0 1.0
NE2 C:HIS59 2.2 28.7 1.0
SG C:CYS37 2.7 41.5 1.0
CE1 C:HIS59 2.7 30.2 1.0
CG C:ASP150 3.2 35.8 1.0
O2 C:EDO354 3.2 44.1 1.0
OG C:SER39 3.2 49.7 1.0
C2 C:EDO354 3.4 48.6 1.0
CD2 C:HIS59 3.4 29.6 1.0
O C:HOH447 3.5 31.7 1.0
CB C:CYS37 3.6 26.1 1.0
OD1 C:ASP150 3.8 34.9 1.0
ND1 C:HIS59 3.9 30.6 1.0
C1 C:EDO354 4.0 55.1 1.0
CG C:HIS59 4.3 26.9 1.0
CB C:SER39 4.3 36.9 1.0
CB C:ASP150 4.4 23.4 1.0
CE C:MET151 4.6 15.6 1.0
OE2 C:GLU60 4.6 36.7 1.0
CD C:GLU60 4.9 33.2 1.0
O C:HOH414 5.0 26.6 1.0
O1 C:EDO354 5.0 47.1 1.0

Zinc binding site 5 out of 6 in 3fsr

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Zinc binding site 5 out of 6 in the 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 5 of 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:Zn355

b:23.6
occ:0.56
O C:HIS287 2.7 16.1 1.0
O C:GLY259 2.8 21.1 1.0
OG1 C:THR289 3.0 27.3 1.0
O C:GLY260 3.0 16.0 1.0
O A:HOH388 3.0 26.9 1.0
OH A:TYR99 3.1 24.6 1.0
C C:GLY259 3.4 18.6 1.0
O A:HOH714 3.7 46.3 1.0
C C:GLY260 3.8 15.9 1.0
C C:HIS287 3.9 14.5 1.0
CZ A:TYR99 3.9 29.1 1.0
CB C:THR289 3.9 23.1 1.0
CA C:GLY259 4.0 13.5 1.0
CG1 C:ILE261 4.0 14.6 1.0
N C:THR289 4.1 13.2 1.0
N C:GLY260 4.1 19.7 1.0
O C:HOH357 4.1 10.3 1.0
CB C:HIS287 4.3 17.1 1.0
CE1 A:TYR99 4.4 22.6 1.0
CA C:GLY260 4.4 15.6 1.0
CA C:HIS287 4.6 11.0 1.0
O C:HOH453 4.6 33.0 1.0
CA C:THR289 4.6 15.8 1.0
CE2 A:TYR99 4.8 27.3 1.0
N C:ILE261 4.8 18.3 1.0
N C:LYS288 4.8 10.3 1.0
CD1 C:ILE261 4.9 15.4 1.0
CA C:LYS288 4.9 15.1 1.0
N C:GLY259 5.0 8.1 1.0
C C:LYS288 5.0 16.2 1.0

Zinc binding site 6 out of 6 in 3fsr

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Zinc binding site 6 out of 6 in the 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 6 of 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:Zn353

b:30.9
occ:0.76
O D:HIS287 2.7 14.7 1.0
OG1 D:THR289 2.8 19.4 1.0
O B:HOH627 2.9 37.5 1.0
O D:GLY259 2.9 18.4 1.0
O D:GLY260 2.9 16.0 1.0
O D:HOH654 2.9 29.8 1.0
OH B:TYR99 3.1 22.0 1.0
C D:GLY259 3.5 22.1 1.0
O D:HOH388 3.7 26.4 1.0
C D:GLY260 3.8 23.7 1.0
CB D:THR289 3.8 16.4 1.0
C D:HIS287 3.8 20.7 1.0
CZ B:TYR99 3.9 23.7 1.0
N D:THR289 4.0 17.3 1.0
CG1 D:ILE261 4.0 20.5 1.0
CA D:GLY259 4.0 17.1 1.0
O B:HOH952 4.1 51.1 1.0
N D:GLY260 4.2 14.7 1.0
CB D:HIS287 4.3 14.1 1.0
O D:HOH356 4.3 7.5 1.0
CA D:GLY260 4.4 18.0 1.0
CA D:THR289 4.5 14.7 1.0
CE1 B:TYR99 4.5 22.6 1.0
CA D:HIS287 4.6 19.2 1.0
CE2 B:TYR99 4.7 27.5 1.0
N D:ILE261 4.8 19.4 1.0
N D:LYS288 4.8 18.6 1.0
CD1 D:ILE261 4.8 21.4 1.0
CA D:LYS288 4.8 14.8 1.0
O D:HOH854 4.9 36.9 1.0
C D:LYS288 4.9 17.3 1.0
O B:HOH843 4.9 51.5 1.0
CA D:ILE261 5.0 18.4 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: Sat Sep 26 06:32:41 2020
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