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Zinc in PDB 2b83: A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization

Enzymatic activity of A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization

All present enzymatic activity of A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization:
1.1.1.2;

Protein crystallography data

The structure of A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization, PDB code: 2b83 was solved by E.Goihberg, O.Dym, Israel Structural Proteomics Center (Ispc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.53 / 2.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 79.470, 103.340, 193.307, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 23

Zinc Binding Sites:

The binding sites of Zinc atom in the A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization (pdb code 2b83). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization, PDB code: 2b83:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2b83

Go back to Zinc Binding Sites List in 2b83
Zinc binding site 1 out of 4 in the A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1353

b:36.5
occ:1.00
 OD2 A:ASP150 2.0 26.8 1.0
NE2 A:HIS59 2.3 26.9 1.0
SG A:CYS37 2.5 24.7 1.0
OE2 A:GLU60 2.5 29.0 1.0
CB A:CYS37 2.9 24.0 1.0
CD2 A:HIS59 3.1 25.4 1.0
CG A:ASP150 3.1 22.0 1.0
CE1 A:HIS59 3.3 28.5 1.0
CD A:GLU60 3.5 24.7 1.0
O A:HOH4710 3.7 53.0 1.0
CB A:ASP150 3.8 19.4 1.0
CE A:MET151 3.9 14.9 1.0
CG A:GLU60 3.9 22.5 1.0
O A:HOH4805 4.0 42.6 1.0
OD1 A:ASP150 4.1 22.4 1.0
CG A:HIS59 4.2 26.9 1.0
ND1 A:HIS59 4.3 29.5 1.0
CA A:CYS37 4.4 25.6 1.0
OG A:SER39 4.4 38.2 1.0
O A:HOH4455 4.5 21.7 1.0
OE1 A:GLU60 4.5 26.1 1.0
CB A:SER39 4.5 36.6 1.0
O A:HOH4488 4.7 21.7 1.0
NZ A:LYS346 4.9 17.0 1.0

Zinc binding site 2 out of 4 in 2b83

Go back to Zinc Binding Sites List in 2b83
Zinc binding site 2 out of 4 in the A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2353

b:38.0
occ:1.00
 OD2 B:ASP150 2.1 27.0 1.0
O B:HOH4354 2.2 23.5 1.0
NE2 B:HIS59 2.2 28.2 1.0
SG B:CYS37 2.4 26.5 1.0
OE2 B:GLU60 2.5 28.9 1.0
CB B:CYS37 3.0 25.2 1.0
CE1 B:HIS59 3.1 29.7 1.0
CG B:ASP150 3.2 23.3 1.0
CD2 B:HIS59 3.2 26.2 1.0
CD B:GLU60 3.4 24.2 1.0
CB B:ASP150 3.7 20.9 1.0
CG B:GLU60 3.8 22.7 1.0
CE B:MET151 3.9 19.3 1.0
ND1 B:HIS59 4.2 28.6 1.0
OD1 B:ASP150 4.2 25.1 1.0
CG B:HIS59 4.2 27.2 1.0
OG B:SER39 4.3 38.7 1.0
OE1 B:GLU60 4.4 21.6 1.0
O B:HOH4606 4.4 44.1 1.0
CA B:CYS37 4.4 25.7 1.0
CB B:SER39 4.6 39.0 1.0
O B:HOH4544 4.7 28.4 1.0
O B:HOH4438 4.9 25.6 1.0
NZ B:LYS346 4.9 16.2 1.0

Zinc binding site 3 out of 4 in 2b83

Go back to Zinc Binding Sites List in 2b83
Zinc binding site 3 out of 4 in the A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn3353

b:33.0
occ:1.00
 OD2 C:ASP150 2.0 23.3 1.0
NE2 C:HIS59 2.2 28.9 1.0
SG C:CYS37 2.4 26.5 1.0
OE2 C:GLU60 2.4 26.8 1.0
CE1 C:HIS59 2.6 30.8 1.0
CB C:CYS37 2.9 24.7 1.0
CG C:ASP150 3.1 21.5 1.0
CD2 C:HIS59 3.4 30.5 1.0
CD C:GLU60 3.4 25.0 1.0
CB C:ASP150 3.7 20.0 1.0
O C:HOH4709 3.8 34.9 1.0
ND1 C:HIS59 3.8 32.0 1.0
CG C:GLU60 3.8 24.6 1.0
CE C:MET151 3.8 20.0 1.0
OG C:SER39 4.1 40.4 1.0
OD1 C:ASP150 4.2 24.9 1.0
CG C:HIS59 4.2 29.5 1.0
CA C:CYS37 4.4 24.9 1.0
OE1 C:GLU60 4.5 22.9 1.0
O C:HOH4552 4.6 24.9 1.0
O C:HOH4391 4.8 22.4 1.0
CB C:SER39 4.8 37.3 1.0

Zinc binding site 4 out of 4 in 2b83

Go back to Zinc Binding Sites List in 2b83
Zinc binding site 4 out of 4 in the A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of A Single Amino Acid Substitution in the Clostridium Beijerinckii Alcohol Dehydrogenase Is Critical For Thermostabilization within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn4353

b:36.8
occ:1.00
 OD2 D:ASP150 2.1 33.2 1.0
NE2 D:HIS59 2.3 37.6 1.0
OE2 D:GLU60 2.4 28.1 1.0
SG D:CYS37 2.4 29.7 1.0
CB D:CYS37 2.9 29.1 1.0
CE1 D:HIS59 2.9 36.2 1.0
CG D:ASP150 3.1 29.5 1.0
CD2 D:HIS59 3.3 36.5 1.0
CD D:GLU60 3.4 25.8 1.0
O D:HOH4942 3.6 37.5 1.0
CB D:ASP150 3.7 27.6 1.0
CG D:GLU60 3.8 25.9 1.0
CE D:MET151 3.9 18.3 1.0
ND1 D:HIS59 4.0 37.8 1.0
OD1 D:ASP150 4.1 34.5 1.0
O D:HOH4514 4.2 44.6 1.0
OG D:SER39 4.2 44.0 1.0
CG D:HIS59 4.3 36.2 1.0
CA D:CYS37 4.4 31.3 1.0
OE1 D:GLU60 4.4 26.6 1.0
O D:HOH4637 4.5 30.8 1.0
O D:HOH4435 4.8 24.9 1.0
CB D:SER39 5.0 41.2 1.0

Reference:

E.Goihberg, O.Dym, S.Tel-Or, I.Levin, M.Peretz, Y.Burstein. A Single Proline Substitution Is Critical For the Thermostabilization of Clostridium Beijerinckii Alcohol Dehydrogenase. Proteins V. 66 196 2006.
ISSN: ISSN 0887-3585
PubMed: 17063493
DOI: 10.1002/PROT.21170
Page generated: Wed Oct 16 21:56:04 2024

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