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Zinc in PDB 6fzc: Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant L184F/L360F

Enzymatic activity of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant L184F/L360F

All present enzymatic activity of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant L184F/L360F:
3.1.1.3;

Protein crystallography data

The structure of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant L184F/L360F, PDB code: 6fzc was solved by S.Gihaz, M.Kanteev, 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 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.140, 71.193, 113.946, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 23.7

Other elements in 6fzc:

The structure of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant L184F/L360F 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 L184F/L360F (pdb code 6fzc). 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 L184F/L360F, PDB code: 6fzc:

Zinc binding site 1 out of 1 in 6fzc

Go back to Zinc Binding Sites List in 6fzc
Zinc binding site 1 out of 1 in the Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant L184F/L360F


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 L184F/L360F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:17.1
occ:1.00
 OD2 A:ASP239 1.9 10.4 1.0
NE2 A:HIS88 1.9 15.6 1.0
OD1 A:ASP62 2.1 11.0 1.0
NE2 A:HIS82 2.3 10.6 1.0
OD2 A:ASP62 2.7 16.5 1.0
CG A:ASP62 2.7 12.1 1.0
CG A:ASP239 2.8 11.7 1.0
CD2 A:HIS88 2.8 12.4 1.0
CE1 A:HIS88 3.0 17.1 1.0
OD1 A:ASP239 3.0 13.1 1.0
CD2 A:HIS82 3.3 11.1 1.0
CE1 A:HIS82 3.3 11.6 1.0
CG A:HIS88 4.0 14.1 1.0
ND1 A:HIS88 4.0 12.5 1.0
OG A:SER59 4.2 15.4 1.0
CB A:ASP239 4.2 10.7 1.0
CB A:ASP62 4.2 15.4 1.0
ND1 A:HIS82 4.4 10.0 1.0
CG A:HIS82 4.4 9.6 1.0
CD1 A:TRP61 4.6 10.5 1.0
CD2 A:HIS86 4.7 9.4 1.0
CZ2 A:TRP212 4.7 14.7 1.0
O A:HOH517 4.8 18.2 1.0
O A:ASP239 4.8 20.8 1.0
CA A:ASP62 4.8 16.9 1.0
N A:ASP62 4.9 14.9 1.0
CB A:HIS86 4.9 7.6 1.0
CG A:HIS86 5.0 10.4 1.0

Reference:

S.Gihaz, M.Kanteev, Y.Pazy, A.Fishman. Filling the Void: Introducing Aromatic Interactions Into Solvent Tunnels to Enhance Lipase Stability in Methanol. Appl.Environ.Microbiol. V. 84 2018.
ISSN: ESSN 1098-5336
PubMed: 30217852
DOI: 10.1128/AEM.02143-18
Page generated: Mon Oct 28 21:32:06 2024

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