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7DAN

Structure of the Ca2+-bound wild-type peptidylarginine deiminase type III (PAD3)

Summary for 7DAN
Entry DOI10.2210/pdb7dan/pdb
Related7D4Y 7D56 7D5R 7D5V 7D8N
DescriptorProtein-arginine deiminase type-3, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
Functional Keywordspeptidylarginie deiminase, citrullination, post-translational modification, enzyme, active form, calcium, isozyme, hydrolase
Biological sourceHomo sapiens (Human)
Total number of polymer chains3
Total formula weight226403.43
Authors
Sawata, M.,Unno, M. (deposition date: 2020-10-16, release date: 2021-06-02, Last modification date: 2023-11-29)
Primary citationFunabashi, K.,Sawata, M.,Nagai, A.,Akimoto, M.,Mashimo, R.,Takahara, H.,Kizawa, K.,Thompson, P.R.,Ite, K.,Kitanishi, K.,Unno, M.
Structures of human peptidylarginine deiminase type III provide insights into substrate recognition and inhibitor design.
Arch.Biochem.Biophys., 708:108911-108911, 2021
Cited by
PubMed: 33971157
DOI: 10.1016/j.abb.2021.108911
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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