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7D5V

Structure of the C646A mutant of peptidylarginine deiminase type III (PAD3)

Summary for 7D5V
Entry DOI10.2210/pdb7d5v/pdb
Related7D4Y 7D56 7D5R
DescriptorProtein-arginine deiminase type-3, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total)
Functional Keywordspeptidylarginine deiminase, isozyme, mutant, citrullination, post-translational modification, enzyme, cytosolic protein, hydrolase
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight151882.53
Authors
Akimoto, M.,Mashimo, R.,Unno, M. (deposition date: 2020-09-28, 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 (2.102 Å)
Structure validation

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