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Atomistry » Calcium » PDB 4fbt-4fs8 » 4fdm » |
Calcium in PDB 4fdm: Crystallization and 3D Structure Elucidation of Thermostable L2 Lipase From Thermophilic Locally Isolated Bacillus Sp. L2.Enzymatic activity of Crystallization and 3D Structure Elucidation of Thermostable L2 Lipase From Thermophilic Locally Isolated Bacillus Sp. L2.
All present enzymatic activity of Crystallization and 3D Structure Elucidation of Thermostable L2 Lipase From Thermophilic Locally Isolated Bacillus Sp. L2.:
3.1.1.3; Protein crystallography data
The structure of Crystallization and 3D Structure Elucidation of Thermostable L2 Lipase From Thermophilic Locally Isolated Bacillus Sp. L2., PDB code: 4fdm
was solved by
R.N.Z.R.A.Rahman,
F.M.Shariff,
A.B.Salleh,
M.B.Basri,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4fdm:
The structure of Crystallization and 3D Structure Elucidation of Thermostable L2 Lipase From Thermophilic Locally Isolated Bacillus Sp. L2. also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystallization and 3D Structure Elucidation of Thermostable L2 Lipase From Thermophilic Locally Isolated Bacillus Sp. L2.
(pdb code 4fdm). 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 Crystallization and 3D Structure Elucidation of Thermostable L2 Lipase From Thermophilic Locally Isolated Bacillus Sp. L2., PDB code: 4fdm: Calcium binding site 1 out of 1 in 4fdmGo back to Calcium Binding Sites List in 4fdm
Calcium binding site 1 out
of 1 in the Crystallization and 3D Structure Elucidation of Thermostable L2 Lipase From Thermophilic Locally Isolated Bacillus Sp. L2.
Mono view Stereo pair view
Reference:
R.N.Abd Rahman,
F.M.Shariff,
M.Basri,
A.B.Salleh.
3D Structure Elucidation of Thermostable L2 Lipase From Thermophilic Bacillus Sp. L2. Int.J.Mol.Sci. V. 13 9207 2012.
Page generated: Sat Dec 12 04:46:17 2020
ISSN: ISSN 1422-0067 PubMed: 22942761 DOI: 10.3390/IJMS13079207 |
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