Calcium in PDB 6fza: Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Methanol Stable Variant A187F

Enzymatic activity of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Methanol Stable Variant A187F

All present enzymatic activity of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Methanol Stable Variant A187F:
3.1.1.3;

Protein crystallography data

The structure of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Methanol Stable Variant A187F, PDB code: 6fza 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) 38.21 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.471, 71.260, 112.223, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 23.1

Other elements in 6fza:

The structure of Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Methanol Stable Variant A187F 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 Methanol Stable Variant A187F (pdb code 6fza). 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 Methanol Stable Variant A187F, PDB code: 6fza:

Calcium binding site 1 out of 1 in 6fza

Go back to Calcium Binding Sites List in 6fza
Calcium binding site 1 out of 1 in the Crystal Structure of Lipase From Geobacillus Stearothermophilus T6 Methanol Stable Variant A187F


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 Methanol Stable Variant A187F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca402

b:21.8
occ:1.00
 OE2 A:GLU361 2.3 13.7 1.0
O A:HOH667 2.3 25.9 1.0
O A:GLY287 2.3 30.8 1.0
O A:PRO367 2.5 18.9 1.0
OD2 A:ASP366 2.6 22.4 1.0
CD A:GLU361 3.3 17.1 1.0
C A:GLY287 3.3 22.3 1.0
CG A:GLU361 3.6 12.4 1.0
C A:PRO367 3.7 19.7 1.0
CG A:ASP366 3.8 24.7 1.0
CA A:GLY287 3.9 20.2 1.0
NH2 A:ARG272 3.9 21.6 1.0
N A:MET288 4.3 14.1 1.0
CB A:ASN368 4.3 21.8 1.0
OE1 A:GLU361 4.4 15.9 1.0
OD1 A:ASP366 4.4 29.2 1.0
CA A:ASN368 4.4 16.8 1.0
N A:ASN368 4.5 17.4 1.0
CA A:MET288 4.6 15.0 1.0
C A:MET288 4.6 14.3 1.0
N A:PRO367 4.6 13.7 1.0
CA A:PRO367 4.7 16.8 1.0
N A:ASN289 4.7 17.4 1.0
CB A:ASP366 4.8 15.4 1.0
CG A:ASN368 4.8 25.2 1.0
C A:ASP366 4.8 15.8 1.0
ND2 A:ASN368 4.9 24.0 1.0
OD2 A:ASP358 4.9 22.8 1.0
CD A:PRO367 4.9 11.6 1.0
O A:HOH632 4.9 34.6 1.0
CZ A:ARG272 5.0 22.2 1.0
O A:HOH540 5.0 33.8 1.0
O A:MET288 5.0 15.3 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: Sat Dec 12 06:07:42 2020

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