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Zinc in PDB 5e2j: Crystal Structure of Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius

Enzymatic activity of Crystal Structure of Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius

All present enzymatic activity of Crystal Structure of Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius:
3.2.1.4;

Protein crystallography data

The structure of Crystal Structure of Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius, PDB code: 5e2j was solved by Y.Y.Hsiao, H.J.Wang, C.P.Tseng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.96 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.421, 144.374, 158.704, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 23.7

Other elements in 5e2j:

The structure of Crystal Structure of Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius (pdb code 5e2j). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius, PDB code: 5e2j:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5e2j

Go back to Zinc Binding Sites List in 5e2j
Zinc binding site 1 out of 2 in the Crystal Structure of Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius


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 Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn602

b:77.7
occ:1.00
ND1 A:HIS122 2.1 71.7 1.0
NE2 A:HIS142 2.2 68.1 1.0
SG A:CYS121 2.4 83.7 1.0
SG A:CYS104 2.4 62.7 1.0
CE1 A:HIS122 2.8 69.6 1.0
CD2 A:HIS142 3.0 66.6 1.0
CG A:HIS122 3.2 74.6 1.0
CB A:CYS121 3.4 66.3 1.0
CE1 A:HIS142 3.4 66.0 1.0
CB A:CYS104 3.5 70.7 1.0
O A:CYS121 3.6 62.9 1.0
CB A:HIS122 3.7 78.2 1.0
C A:CYS121 3.8 68.9 1.0
NE2 A:HIS122 4.0 69.2 1.0
CD2 A:HIS122 4.2 73.3 1.0
CA A:CYS121 4.2 72.1 1.0
CA A:CYS104 4.2 73.4 1.0
CG A:HIS142 4.2 66.1 1.0
N A:HIS122 4.3 73.5 1.0
ND1 A:HIS142 4.4 65.2 1.0
O A:HOH734 4.4 75.2 1.0
CB A:TYR147 4.5 72.8 1.0
N A:GLY105 4.5 91.2 1.0
O A:TYR147 4.5 65.8 1.0
CA A:HIS122 4.6 79.9 1.0
CD1 A:TYR147 4.8 71.5 1.0
C A:CYS104 4.9 80.6 1.0
CG A:TYR147 4.9 74.4 1.0
N A:CYS121 5.0 77.2 1.0

Zinc binding site 2 out of 2 in 5e2j

Go back to Zinc Binding Sites List in 5e2j
Zinc binding site 2 out of 2 in the Crystal Structure of Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius


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 Single Mutant Thermostable Endoglucanase (D468A) From Alicyclobacillus Acidocaldarius within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn602

b:45.7
occ:1.00
NE2 B:HIS142 2.2 43.6 1.0
ND1 B:HIS122 2.2 46.9 1.0
SG B:CYS104 2.3 45.9 1.0
SG B:CYS121 2.4 46.3 1.0
CE1 B:HIS122 3.0 47.3 1.0
CE1 B:HIS142 3.0 43.2 1.0
CB B:CYS104 3.2 39.8 1.0
CG B:HIS122 3.2 50.9 1.0
CD2 B:HIS142 3.2 39.2 1.0
CB B:CYS121 3.3 46.7 1.0
O B:CYS121 3.4 46.1 1.0
C B:CYS121 3.6 47.0 1.0
CA B:CYS104 3.6 41.6 1.0
CB B:HIS122 3.6 55.6 1.0
N B:GLY105 4.0 46.8 1.0
CA B:CYS121 4.0 44.4 1.0
N B:HIS122 4.1 47.7 1.0
NE2 B:HIS122 4.2 44.4 1.0
ND1 B:HIS142 4.2 45.2 1.0
CD2 B:HIS122 4.3 47.6 1.0
C B:CYS104 4.3 44.2 1.0
CG B:HIS142 4.3 43.0 1.0
CA B:HIS122 4.5 52.8 1.0
N B:CYS121 4.7 50.3 1.0
CB B:PRO228 4.8 45.2 1.0
N B:CYS104 4.9 41.7 1.0
O B:LEU103 5.0 41.9 1.0

Reference:

H.J.Wang, Y.Y.Hsiao, Y.P.Chen, T.Y.Ma, C.P.Tseng. Polarity Alteration of A Calcium Site Induces A Hydrophobic Interaction Network and Enhances CEL9A Endoglucanase Thermostability. Appl.Environ.Microbiol. V. 82 1662 2016.
ISSN: ESSN 1098-5336
PubMed: 26729722
DOI: 10.1128/AEM.03326-15
Page generated: Sun Oct 27 14:57:44 2024

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