Atomistry » Zinc » PDB 3flf-3fuk » 3fsr
Atomistry »
  Zinc »
    PDB 3flf-3fuk »
      3fsr »

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

Other elements in 3fsr:

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 also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

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

Go back to Zinc Binding Sites List in 3fsr
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

Go back to Zinc Binding Sites List in 3fsr
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

Go back to Zinc Binding Sites List in 3fsr
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

Go back to Zinc Binding Sites List in 3fsr
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

Go back to Zinc Binding Sites List in 3fsr
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: Thu Oct 24 13:23:15 2024

Last articles

Mg in 2X3J
Mg in 2X5F
Mg in 2X4D
Mg in 2X2R
Mg in 2X2E
Mg in 2X2F
Mg in 2X2Q
Mg in 2X21
Mg in 2X1A
Mg in 2X1Z
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy