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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) |
![]() | Funabashi, K. / Sawata, M. / Nagai, A. / Akimoto, M. / Mashimo, R. / Takahara, H. / Kizawa, K. / Thompson, P.R. / Ite, K. / Kitanishi, K. / Unno, M. |
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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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![]() | 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 |