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Zinc in PDB 1bxz: Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii

Enzymatic activity of Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii

All present enzymatic activity of Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii:
1.1.1.2;

Protein crystallography data

The structure of Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii, PDB code: 1bxz was solved by C.Li, J.Heatwole, S.Soelaiman, M.Shoham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.99
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 80.450, 123.080, 168.030, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 26.4

Other elements in 1bxz:

The structure of Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms
Chlorine (Cl) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii (pdb code 1bxz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii, PDB code: 1bxz:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1bxz

Go back to Zinc Binding Sites List in 1bxz
Zinc binding site 1 out of 4 in the Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn354

b:26.1
occ:1.00
 N A:THR38 2.9 48.5 1.0
SG A:CYS37 2.9 48.1 1.0
CA A:CYS37 3.0 46.0 1.0
CB A:CYS37 3.4 47.2 1.0
C A:CYS37 3.4 46.8 1.0
CE A:LYS346 3.5 34.1 1.0
OG1 A:THR38 3.8 53.3 1.0
O A:PRO36 3.8 35.6 1.0
CD A:LYS346 4.0 33.6 1.0
CA A:THR38 4.0 51.2 1.0
CB A:THR38 4.1 51.1 1.0
N A:CYS37 4.2 42.2 1.0
NZ A:LYS346 4.2 31.2 1.0
SD A:MET151 4.3 25.2 1.0
C A:PRO36 4.4 39.7 1.0
SD A:MET337 4.5 47.0 1.0
OE2 A:GLU60 4.5 35.2 1.0
CG A:PRO177 4.5 36.2 1.0
CE A:MET151 4.6 30.6 1.0
O A:CYS37 4.6 46.7 1.0
N A:SER39 4.9 52.3 1.0

Zinc binding site 2 out of 4 in 1bxz

Go back to Zinc Binding Sites List in 1bxz
Zinc binding site 2 out of 4 in the Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn354

b:27.8
occ:1.00
 SG B:CYS37 2.8 51.4 1.0
CA B:CYS37 3.0 46.3 1.0
N B:THR38 3.2 49.5 1.0
CB B:CYS37 3.3 48.7 1.0
CE B:LYS346 3.4 32.7 1.0
OE2 B:GLU60 3.6 38.0 1.0
C B:CYS37 3.6 47.4 1.0
SD B:MET151 3.9 30.5 1.0
O B:PRO36 3.9 41.9 1.0
NZ B:LYS346 4.0 30.3 1.0
N B:CYS37 4.2 44.8 1.0
OG1 B:THR38 4.3 54.8 1.0
CD B:LYS346 4.3 34.0 1.0
OD2 B:ASP150 4.4 43.4 1.0
CE B:MET151 4.4 31.2 1.0
CA B:THR38 4.5 52.6 1.0
C B:PRO36 4.5 42.2 1.0
CD B:GLU60 4.5 40.1 1.0
CB B:THR38 4.6 52.9 1.0
O B:CYS37 4.8 47.7 1.0
OE1 B:GLU60 4.8 40.7 1.0
CG B:PRO177 4.9 37.0 1.0
N B:SER39 5.0 54.1 1.0

Zinc binding site 3 out of 4 in 1bxz

Go back to Zinc Binding Sites List in 1bxz
Zinc binding site 3 out of 4 in the Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn354

b:26.9
occ:1.00
 SG C:CYS37 2.6 61.7 1.0
CB C:CYS37 2.6 54.5 1.0
CA C:CYS37 2.7 51.9 1.0
CE C:LYS346 3.0 37.0 1.0
OE2 C:GLU60 3.1 44.7 1.0
N C:THR38 3.4 54.0 1.0
NZ C:LYS346 3.4 37.4 1.0
O C:PRO36 3.5 48.6 1.0
C C:CYS37 3.5 52.6 1.0
SD C:MET151 3.9 34.0 1.0
N C:CYS37 3.9 48.3 1.0
CD C:LYS346 4.0 38.3 1.0
CD C:GLU60 4.1 43.5 1.0
C C:PRO36 4.1 46.0 1.0
OE1 C:GLU60 4.4 47.4 1.0
CE C:MET151 4.6 33.1 1.0
OD2 C:ASP150 4.6 45.4 1.0
CA C:THR38 4.7 55.1 1.0
O C:CYS37 4.7 53.2 1.0
SD C:MET337 4.9 63.1 1.0
N C:SER39 4.9 57.2 1.0
OG1 C:THR38 5.0 56.1 1.0
CB C:THR38 5.0 55.6 1.0

Zinc binding site 4 out of 4 in 1bxz

Go back to Zinc Binding Sites List in 1bxz
Zinc binding site 4 out of 4 in the Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex From Thermoanaerobacter Brockii within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn354

b:28.0
occ:1.00
 SG D:CYS37 2.6 57.1 1.0
N D:THR38 2.8 50.1 1.0
CA D:CYS37 2.8 49.6 1.0
CB D:CYS37 3.0 52.0 1.0
C D:CYS37 3.3 50.3 1.0
CE D:LYS346 3.8 35.9 1.0
CA D:THR38 4.0 52.4 1.0
SD D:MET151 4.1 31.0 1.0
OE2 D:GLU60 4.2 42.0 1.0
O D:PRO36 4.2 44.8 1.0
N D:CYS37 4.2 46.8 1.0
OG1 D:THR38 4.2 56.6 1.0
CB D:THR38 4.2 54.4 1.0
N D:SER39 4.5 54.0 1.0
O D:CYS37 4.5 52.1 1.0
NZ D:LYS346 4.5 38.2 1.0
CE D:MET151 4.5 30.6 1.0
CD D:LYS346 4.6 36.0 1.0
C D:PRO36 4.6 44.2 1.0
OD2 D:ASP150 4.8 41.9 1.0
C D:THR38 4.8 52.8 1.0
CG D:PRO177 4.9 36.1 1.0

Reference:

C.Li, J.Heatwole, S.Soelaiman, M.Shoham. Crystal Structure of A Thermophilic Alcohol Dehydrogenase Substrate Complex Suggests Determinants of Substrate Specificity and Thermostability. Proteins V. 37 619 1999.
ISSN: ISSN 0887-3585
PubMed: 10651277
DOI: 10.1002/(SICI)1097-0134(19991201)37:4<619::AID-PROT12>3.0.CO;2-H
Page generated: Sat Oct 12 22:47:37 2024

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