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-Structure paper
Title | Structures of human peptidylarginine deiminase type III provide insights into substrate recognition and inhibitor design. |
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Journal, issue, pages | Arch. Biochem. Biophys., Vol. 708, Page 108911-108911, Year 2021 |
Publish date | Sep 24, 2020 (structure data deposition date) |
Authors | Funabashi, K. / Sawata, M. / Nagai, A. / Akimoto, M. / Mashimo, R. / Takahara, H. / Kizawa, K. / Thompson, P.R. / Ite, K. / Kitanishi, K. / Unno, M. |
External links | Arch. Biochem. Biophys. / PubMed:33971157 |
Methods | X-ray diffraction |
Resolution | 2.102 - 3.175 Å |
Structure data | PDB-7d4y: PDB-7d56: PDB-7d5r: PDB-7d5v: PDB-7d8n: PDB-7dan: |
Chemicals | ChemComp-HOH: ChemComp-BFB: ChemComp-CA: ChemComp-CL: ChemComp-EDO: ChemComp-GOL: |
Source |
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Keywords | HYDROLASE / post-translational modification / citrullination / calcium-dependent / calcium-binding / CYTOSOLIC PROTEIN / Posttransrational modification / calcium metabolism / deimination / peptidylarginine deiminase / enzyme / isozyme / mutant / inactive / calcium ion / peptidylarginie deiminase / active form / calcium |