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TitleA Peptide Bond from the Inter-lobe Segment in the Bilobal Lactoferrin Acts as a Preferred Site for Cleavage for Serine Proteases to Generate the Perfect C-lobe: Structure of the Pepsin Hydrolyzed Lactoferrin C-lobe at 2.28 angstrom Resolution.
Journal, issue, pagesProtein J., Vol. 40, Page 857-866, Year 2021
Publish dateJul 18, 2021 (structure data deposition date)
AuthorsSingh, J. / Maurya, A. / Singh, P.K. / Viswanathan, V. / Ahmad, M.I. / Sharma, P. / Sharma, S. / Singh, T.P.
External linksProtein J. / PubMed:34734372
MethodsX-ray diffraction
Resolution2.277 Å
Structure data

PDB-7fdw:
Crystal structure of pepsin cleaved lactoferrin C-lobe at 2.28 A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.277 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-CO3:
CARBONATE ION

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

Source
  • bos taurus (domestic cattle)
KeywordsHYDROLASE / C lobe of lactoferrin

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