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Atomistry » Calcium » PDB 5odc-5oyj » 5onq | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 5odc-5oyj » 5onq » |
Calcium in PDB 5onq: Alzheimer'S Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd- Substituted ThermolysinEnzymatic activity of Alzheimer'S Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd- Substituted Thermolysin
All present enzymatic activity of Alzheimer'S Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd- Substituted Thermolysin:
3.4.24.27; Protein crystallography data
The structure of Alzheimer'S Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd- Substituted Thermolysin, PDB code: 5onq
was solved by
J.P.Leite,
L.Gales,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5onq:
The structure of Alzheimer'S Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd- Substituted Thermolysin also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Alzheimer'S Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd- Substituted Thermolysin
(pdb code 5onq). 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 Alzheimer'S Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd- Substituted Thermolysin, PDB code: 5onq: Calcium binding site 1 out of 1 in 5onqGo back to Calcium Binding Sites List in 5onq
Calcium binding site 1 out
of 1 in the Alzheimer'S Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd- Substituted Thermolysin
Mono view Stereo pair view
Reference:
J.P.Leite,
L.Gales.
Alzheimer'S A BETA1-40PEPTIDE Degradation By Thermolysin: Evidence of Inhibition By A C-Terminal A Beta Product. Febs Lett. V. 593 128 2019.
Page generated: Mon Jul 15 09:51:46 2024
ISSN: ISSN 1873-3468 PubMed: 30403288 DOI: 10.1002/1873-3468.13285 |
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