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Atomistry » Calcium » PDB 5l0v-5lia » 5l7p | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 5l0v-5lia » 5l7p » |
Calcium in PDB 5l7p: In Silico-Powered Specific Incorporation of Photocaged Dopa at Multiple Protein SitesEnzymatic activity of In Silico-Powered Specific Incorporation of Photocaged Dopa at Multiple Protein Sites
All present enzymatic activity of In Silico-Powered Specific Incorporation of Photocaged Dopa at Multiple Protein Sites:
6.1.1.1; Protein crystallography data
The structure of In Silico-Powered Specific Incorporation of Photocaged Dopa at Multiple Protein Sites, PDB code: 5l7p
was solved by
M.Hauf,
F.Richter,
T.Schneider,
B.M.Martins,
T.Baumann,
P.Durkin,
H.Dobbek,
A.Moeglich,
N.Budisa,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5l7p:
The structure of In Silico-Powered Specific Incorporation of Photocaged Dopa at Multiple Protein Sites also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the In Silico-Powered Specific Incorporation of Photocaged Dopa at Multiple Protein Sites
(pdb code 5l7p). 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 In Silico-Powered Specific Incorporation of Photocaged Dopa at Multiple Protein Sites, PDB code: 5l7p: Calcium binding site 1 out of 1 in 5l7pGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the In Silico-Powered Specific Incorporation of Photocaged Dopa at Multiple Protein Sites
![]() Mono view ![]() Stereo pair view
Reference:
M.Hauf,
F.Richter,
T.Schneider,
T.Faidt,
B.M.Martins,
T.Baumann,
P.Durkin,
H.Dobbek,
K.Jacobs,
A.Moglich,
N.Budisa.
Photoactivatable Mussel-Based Underwater Adhesive Proteins By An Expanded Genetic Code. Chembiochem V. 18 1819 2017.
Page generated: Mon Jul 15 07:21:29 2024
ISSN: ESSN 1439-7633 PubMed: 28650092 DOI: 10.1002/CBIC.201700327 |
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