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Calcium 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:

Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Variant L184F/L360F, PDB code: 6fzc:

Calcium binding site 1 out of 1 in 6fzc

Go back to Calcium Binding Sites List in 6fzc
Calcium 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 Calcium with other atoms in the Ca 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:Ca402

b:63.9
occ:1.00
 O A:GLY287 2.1 45.6 1.0
OE2 A:GLU361 2.3 26.3 1.0
OD2 A:ASP366 2.7 31.9 1.0
O A:PRO367 2.7 18.4 1.0
O A:HOH590 3.1 24.6 1.0
C A:GLY287 3.2 37.7 1.0
CD A:GLU361 3.4 19.3 1.0
CG A:GLU361 3.8 19.3 1.0
CG A:ASP366 3.8 34.8 1.0
C A:PRO367 3.9 21.6 1.0
CA A:GLY287 3.9 28.1 1.0
NH2 A:ARG272 4.1 39.0 1.0
N A:MET288 4.3 38.6 1.0
OE1 A:GLU361 4.5 15.5 1.0
N A:ASN289 4.5 29.4 1.0
CA A:MET288 4.5 31.6 1.0
C A:MET288 4.5 29.1 1.0
OD2 A:ASP358 4.6 30.2 1.0
OD1 A:ASP366 4.6 40.5 1.0
N A:PRO367 4.7 28.5 1.0
CB A:ASP366 4.7 17.4 1.0
CB A:ASN368 4.7 24.9 1.0
N A:ASN368 4.8 20.3 1.0
CD A:PRO367 4.8 23.4 1.0
CA A:ASN368 4.9 23.8 1.0
CA A:PRO367 4.9 23.6 1.0
CG A:PRO367 4.9 20.2 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: Tue Jul 16 07:57:12 2024

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