HB3VAR03 apo headstructure (PfEMP1 A). Determined by electron microscopy at 3.8 Å resolution. Released 2 Aug 2023.
Explore 8C3Y in 3D Show helices and sheets RCSB PDB PDBe
8C3Y contains 44 α-helices and 12 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-41 | 21 | |
| α-helix | 92-96 | 5 | |
| β-strand | 108 | 1 | 1 |
| α-helix | 127 | 1 | |
| β-strand | 128 | 1 | 1 |
| α-helix | 129 | 1 | |
| α-helix | 130-133 | 4 | |
| α-helix | 138-141 | 4 | |
| α-helix | 151-171 | 21 | |
| α-helix | 180-197 | 18 | |
| α-helix | 212-226 | 15 | |
| α-helix | 228-231 | 4 | |
| α-helix | 236-255 | 20 | |
| β-strand | 266-267 | 2 | 2 |
| β-strand | 275-276 | 2 | 2 |
| α-helix | 277-278 | 2 | |
| α-helix | 297-324 | 28 | |
| β-strand | 325-326 | 2 | 3 |
| α-helix | 328-330 | 3 | |
| β-strand | 331-332 | 2 | 3 |
| β-strand | 333 | 1 | 4 |
| β-strand | 339 | 1 | 4 |
| α-helix | 357-388 | 32 | |
| α-helix | 389-393 | 5 | |
| α-helix | 414-417 | 4 | |
| α-helix | 422-430 | 9 | |
| β-strand | 503-509 | 7 | 5 |
| α-helix | 518-522 | 5 | |
| α-helix | 524-527 | 4 | |
| β-strand | 537-543 | 7 | 5 |
| β-strand | 552-557 | 6 | 5 |
| α-helix | 565-567 | 3 | |
| β-strand | 568-570 | 3 | 5 |
| α-helix | 571-592 | 22 | |
| α-helix | 594-597 | 4 | |
| α-helix | 605-630 | 26 | |
| α-helix | 641-643 | 3 | |
| α-helix | 649-653 | 5 | |
| α-helix | 656-658 | 3 | |
| α-helix | 667-685 | 19 | |
| α-helix | 691-712 | 22 | |
| α-helix | 716-718 | 3 | |
| α-helix | 741-743 | 3 | |
| α-helix | 744-762 | 19 | |
| α-helix | 765-768 | 4 | |
| α-helix | 845-847 | 3 | |
| α-helix | 869-891 | 23 | |
| α-helix | 905-923 | 19 | |
| α-helix | 932-951 | 20 | |
| α-helix | 955-957 | 3 | |
| α-helix | 959-961 | 3 | |
| α-helix | 964-966 | 3 | |
| α-helix | 972-993 | 22 | |
| α-helix | 1014-1039 | 26 | |
| α-helix | 1058-1096 | 39 | |
| α-helix | 1113-1125 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PfEMP1 | A | protein | 1260 | Plasmodium falciparum HB3 | A0A0L7KL67 |
>8C3Y_1 PfEMP1 (chains A) MASSASKFSKIVVGNETHKSARNVLEGFAKDIKGKASIDAEKHAYSLKGNLKDAKFNHDF FKIKSDMPGNPCYLDFAFHSNTPGNQREYRHPCARSMNKNLFNLEGAVCTNSKIKGNEEK INGAGACAPYRRRHICDLNLEHIDVHNVQNIHDLLGNVLVTAKYEGESIVEKHPNRGSSE VCTALARSFADIGDIIRGKDLYLGHEQGNNKLEARLKTIFQNIKNKNKSPLDKLSLEQVR EYWWALNREDVWKALTCFADGSEEYFIQSSDKEHSFSSEYCGHEQGNVPTNLDYVPQFLR WFDEWADDFCRIKKIKLENVKNACRDEKKRKYCSLNGFDCTQTIWKKGVLHRSNECTGCL VKCNPYEIWLGNQREAFRKQKEKYENEIKTYVHDTGISNSNINNEYYKEFYKILKNNNYE TANEFIKLLNEGRYCNKKEKIEEEEDIDFTNTNEKGTFYRSDYCQVCPDCGVECKNETCT PKTVIYPDCGKNEKYEPPGDAKNTEINVINSGDKEGYIFEKLSEFCTNENNENGKNYEQW KCYYDNKKNNNKCKMEINIANSKLKNKITSFDEFFDFWVRKLLIDTIKWETELTYCINNT DVTDCNKCNKNCVCFDKWVKQKEDEWTNIMKLFTNKHDIPKKYYLNINDLFDSFFFQVIY KFNEGEAKWNELKENLKKQIASSKANNGTKDSEAAIKVLFNHIKEIATICKDNNTNEGCD PSVDSKTNSCGKNTKAGSDKVISVKQIAQYYKRIAHKQLNERGSRSALKGDASKGTYKKN GTPSNLKEICEITAKHSNDSRRDGEPCTGKDGGQVRVRTKIGTPWTKIVEINKTSYKEVF LPPRRQHMCTSNLEHLNTGNKGLKDGKLAIHSLLGDVLLAAKEQANFIKNKYKRQKASNG FKDKGTICRAIRYSYADLGDIIKGTDLWEANPGEKNTQRRLKTVFGIIKKNMPGIKDNQK YKDDEKNNPPYKLLREDWWEANRDQVWQAMKCAMKNGITCGSSDHTPLDDYIPQKLRWLT EWAEWYCKAQSKEYEKLKEKCKECKGNDQCTQDTPDCEKCKAACKKYGKNIKTWEDQWKV ISSKYKELYKQAEIYAGNGGPGYYNTKVQEEDKPVVDFLYNLYLQNGGKKGPPPDTHPSK SVTAPLKQVATVDTPSTVYSTPEGYIHQEAAMDCKQQHVFCDDNSGGKDDNKQYAFRHQP HDYDEALRCDQRDKPPPESKKVEKAKKEKDENDDGGSHHHHHHGGGSAHIVMVDAYKPTK
Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1. Rajan Raghavan, S.S., Turner, L., Jensen, R.W. et al. Structure (2023) 31:1174-1183.e4. DOI 10.1016/j.str.2023.07.011 · PubMed
Other PDB entries of the same protein (UniProt A0A0L7KL67), best resolution first:
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