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Calcium in PDB 2w22: Activation Mechanism of Bacterial Thermoalkalophilic Lipases

Enzymatic activity of Activation Mechanism of Bacterial Thermoalkalophilic Lipases

All present enzymatic activity of Activation Mechanism of Bacterial Thermoalkalophilic Lipases:
3.1.1.3;

Protein crystallography data

The structure of Activation Mechanism of Bacterial Thermoalkalophilic Lipases, PDB code: 2w22 was solved by C.Carrasco-Lopez, C.Godoy, B.De Las Rivas, G.Fernandez-Lorente, J.M.Palomo, J.M.Guisan, R.Fernandez-Lafuente, J.A.Hermoso, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.18 / 2.20
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.070, 128.080, 127.490, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 22.6

Other elements in 2w22:

The structure of Activation Mechanism of Bacterial Thermoalkalophilic Lipases also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Activation Mechanism of Bacterial Thermoalkalophilic Lipases (pdb code 2w22). 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 Activation Mechanism of Bacterial Thermoalkalophilic Lipases, PDB code: 2w22:

Calcium binding site 1 out of 1 in 2w22

Go back to Calcium Binding Sites List in 2w22
Calcium binding site 1 out of 1 in the Activation Mechanism of Bacterial Thermoalkalophilic Lipases


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Activation Mechanism of Bacterial Thermoalkalophilic Lipases within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca401

b:67.9
occ:1.00
O A:PRO367 2.6 28.6 1.0
O A:GLY287 2.6 33.5 1.0
OD2 A:ASP366 2.9 38.5 1.0
OE2 A:GLU361 3.0 30.2 1.0
O A:HOH2528 3.0 48.7 1.0
O A:HOH2504 3.6 50.9 1.0
C A:GLY287 3.6 32.9 1.0
O A:HOH2289 3.7 49.1 1.0
C A:PRO367 3.8 31.0 1.0
CG A:ASP366 3.9 37.6 1.0
CD A:GLU361 4.0 30.1 1.0
O A:HOH2426 4.1 47.0 1.0
CA A:GLY287 4.1 33.8 1.0
O A:HOH2219 4.3 62.0 1.0
CG A:GLU361 4.3 26.9 1.0
NH2 A:ARG272 4.4 26.0 1.0
CG A:PRO367 4.5 31.8 1.0
N A:PRO367 4.5 31.9 1.0
OD1 A:ASP366 4.6 39.8 1.0
N A:MET288 4.6 31.3 1.0
CA A:PRO367 4.7 31.2 1.0
C A:MET288 4.7 31.2 1.0
CD A:PRO367 4.7 30.2 1.0
N A:ASN368 4.7 30.9 1.0
N A:ASN289 4.7 31.6 1.0
CB A:ASN368 4.7 32.0 1.0
CA A:ASN368 4.7 32.6 1.0
CB A:ASP366 4.8 34.1 1.0
CA A:MET288 4.9 29.8 1.0
C A:ASP366 4.9 31.4 1.0

Reference:

C.Carrasco-Lopez, C.Godoy, B.De Las Rivas, G.Fernandez-Lorente, J.M.Palomo, J.M.Guisan, R.Fernandez-Lafuente, M.Martinez-Ripoll, J.A.Hermoso. Activation of Bacterial Thermoalkalophilic Lipases Is Spurred By Dramatic Structural Rearrangements. J. Biol. Chem. V. 284 4365 2009.
ISSN: ISSN 0021-9258
PubMed: 19056729
DOI: 10.1074/JBC.M808268200
Page generated: Sat Dec 12 03:54:56 2020

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