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Calcium in PDB 4cg0: Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction AnalysisEnzymatic activity of Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis
All present enzymatic activity of Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis:
3.4.21.62; Protein crystallography data
The structure of Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis, PDB code: 4cg0
was solved by
C.G.Frankaer,
O.V.Moroz,
J.P.Turkenburg,
S.I.Aspmo,
M.Thymark,
E.P.Friis,
K.Stahla,
J.E.Nielsen,
K.S.Wilson,
P.Harris,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4cg0:
The structure of Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis
(pdb code 4cg0). 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 Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis, PDB code: 4cg0: Calcium binding site 1 out of 1 in 4cg0Go back to Calcium Binding Sites List in 4cg0
Calcium binding site 1 out
of 1 in the Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis
Mono view Stereo pair view
Reference:
C.G.Frankaer,
O.V.Moroz,
J.P.Turkenburg,
S.I.Aspmo,
M.Thymark,
E.P.Friis,
K.Stahl,
J.E.Nielsen,
K.S.Wilson,
P.Harris.
Analysis of An Industrial Production Suspension of Bacillus Lentus Subtilisin Crystals By Powder Diffraction: A Powerful Quality-Control Tool. Acta Crystallogr.,Sect.D V. 70 1115 2014.
Page generated: Sat Dec 12 04:42:15 2020
ISSN: ISSN 0907-4449 PubMed: 24699655 DOI: 10.1107/S1399004714001497 |
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