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Zinc in PDB 6s3g: Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant A187C/F291C

Enzymatic activity of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant A187C/F291C

All present enzymatic activity of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant A187C/F291C:
3.1.1.3;

Protein crystallography data

The structure of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant A187C/F291C, PDB code: 6s3g was solved by S.Gihaz, Y.Bash, I.Rush, A.Shahar, Y.Pazy, A.Fishman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.48 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.074, 71.315, 113.793, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 20.8

Other elements in 6s3g:

The structure of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant A187C/F291C also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant A187C/F291C (pdb code 6s3g). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant A187C/F291C, PDB code: 6s3g:

Zinc binding site 1 out of 1 in 6s3g

Go back to Zinc Binding Sites List in 6s3g
Zinc binding site 1 out of 1 in the Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant A187C/F291C


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 Lipase From Geobacillus Stearothermophilus T6 Variant A187C/F291C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:21.6
occ:1.00
 OD2 A:ASP239 1.9 16.5 1.0
NE2 A:HIS82 2.1 18.3 1.0
OD1 A:ASP62 2.1 18.0 1.0
NE2 A:HIS88 2.2 18.6 1.0
CG A:ASP239 2.6 17.1 1.0
CG A:ASP62 2.8 22.2 1.0
OD1 A:ASP239 2.8 18.4 1.0
OD2 A:ASP62 2.9 21.9 1.0
CD2 A:HIS88 3.0 22.3 1.0
CD2 A:HIS82 3.0 16.9 1.0
CE1 A:HIS82 3.0 21.9 1.0
CE1 A:HIS88 3.2 17.4 1.0
OG A:SER59 3.9 17.6 1.0
CB A:ASP239 4.1 18.8 1.0
ND1 A:HIS82 4.2 18.6 1.0
CG A:HIS82 4.2 18.9 1.0
CG A:HIS88 4.2 21.9 1.0
ND1 A:HIS88 4.3 22.3 1.0
CB A:ASP62 4.3 16.6 1.0
CD1 A:TRP61 4.4 14.4 1.0
O A:HOH610 4.6 22.2 1.0
CD2 A:HIS86 4.6 23.0 1.0
N A:ASP62 4.8 16.1 1.0
O A:ASP239 4.8 21.4 1.0
CA A:ASP62 4.9 15.3 1.0
CB A:HIS86 4.9 18.2 1.0
CG A:HIS86 4.9 22.9 1.0
CB A:SER59 5.0 17.4 1.0
CZ2 A:TRP212 5.0 22.4 1.0

Reference:

S.Gihaz, Y.Bash, I.Rush, A.Shahar, Y.Pazy, A.Fishman. Bridges to Stability: Engineering Disulfide Bonds Towards Enhanced Lipase Biodiesel Synthesis Chemcatchem 2019.
ISSN: ESSN 1867-3899
DOI: 10.1002/CCTC.201901369
Page generated: Tue Oct 29 07:01:14 2024

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