HB3VAR03 apo headstructure (PfEMP1 A) complexed with EPCR. Determined by electron microscopy at 3.2 Å resolution. Released 16 Aug 2023.
Explore 8C44 in 3D Show helices and sheets RCSB PDB PDBe
8C44 contains 29 α-helices and 22 β-strands across 2 chains. 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 |
|---|---|---|---|
| β-strand | 504-506 | 3 | 1 |
| β-strand | 540-542 | 3 | 1 |
| β-strand | 552-554 | 3 | 1 |
| β-strand | 568-570 | 3 | 1 |
| α-helix | 571-593 | 23 | |
| α-helix | 607-630 | 24 | |
| β-strand | 646 | 1 | 2 |
| α-helix | 647-659 | 13 | |
| α-helix | 665-682 | 18 | |
| β-strand | 694 | 1 | 2 |
| α-helix | 695-714 | 20 | |
| α-helix | 744-762 | 19 | |
| α-helix | 765-768 | 4 | |
| α-helix | 772-774 | 3 | |
| α-helix | 823-825 | 3 | |
| β-strand | 826-828 | 3 | 3 |
| β-strand | 839-841 | 3 | 3 |
| α-helix | 842 | 1 | |
| α-helix | 843-846 | 4 | |
| α-helix | 869-891 | 23 | |
| α-helix | 904-923 | 20 | |
| α-helix | 932-949 | 18 | |
| α-helix | 972-981 | 10 | |
| α-helix | 984-989 | 6 | |
| β-strand | 1003 | 1 | 4 |
| β-strand | 1006 | 1 | 4 |
| α-helix | 1009-1011 | 3 | |
| α-helix | 1014-1034 | 21 | |
| β-strand | 1066 | 1 | 5 |
| β-strand | 1068 | 1 | 5 |
| α-helix | 1070-1095 | 26 | |
| α-helix | 1113-1124 | 12 | |
| α-helix | 1162-1169 | 8 | |
| β-strand | 1179 | 1 | 6 |
| β-strand | 1194 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-21 | 12 | 7 |
| β-strand | 24-33 | 10 | 7 |
| β-strand | 36-44 | 9 | 7 |
| β-strand | 49-52 | 4 | 7 |
| α-helix | 59-86 | 28 | |
| β-strand | 93-102 | 10 | 7 |
| α-helix | 110 | 1 | |
| β-strand | 111-118 | 8 | 7 |
| β-strand | 121-127 | 7 | 7 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-135 | 4 | 7 |
| α-helix | 142-153 | 12 | |
| α-helix | 155-158 | 4 | |
| α-helix | 160-163 | 4 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-175 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PfEMP1 | A | protein | 1259 | Plasmodium falciparum HB3 | A0A0L7KL67 |
| Endothelial protein C receptor | C | protein | 168 | Homo sapiens | Q9UNN8 (AlphaFold model) |
>8C44_1 PfEMP1 (chains A) MASSASKFSKIVVGNETHKSARNVLEGFAKDIKGKASIDAEKHAYSLKGNLKDAKFNHDF FKIKSDMPGNPCYLDFAFHSNTPGNQREYRHPCARSMNKNLFNLEGAVCTNSKIKGNEEK INGAGACAPYRRRHICDLNLEHIDVHNVQNIHDLLGNVLVTAKYEGESIVEKHPNRGSSE VCTALARSFADIGDIIRGKDLYLGHEQGNNKLEARLKTIFQNIKNKNKSPLDKLSLEQVR EYWWALNREDVWKALTCFADGSEEYFIQSSDKEHSFSSEYCGHEQGNVPTNLDYVPQFLR WFDEWADDFCRIKKIKLENVKNACRDEKKRKYCSLNGFDCTQTIWKKGVLHRSNECTGCL VKCNPYEIWLGNQREAFRKQKEKYENEIKTYVHDTGISNSNINNEYYKEFYKILKNNNYE TANEFIKLLNEGRYCNKKEKIEEEEDIDFTNTNEKGTFYRSDYCQVCPDCGVECKNETCT PKTVIYPDCGKNEKYEPPGDAKNTEINVINSGDKEGYIFEKLSEFCTNENTENINNYEQW KCYYDNKKNNNKCKMEINIANSKLKNKVTSFDEFFDFWVRKLLIDTIKWETELTYCINNT DKFWCNKCNKNCVCFDKWVKQKEDEWTNIMKLFTNKHDIPKKYYLNINDLFDSFFFQVIY KFNEGEAKWNELKENLKKQIASSKANNGTKDSEAAIKVLFNHIKEIATICKDNNTNEGCD PSVDSKTNSCGKNTKAGSDKVISVKQIAQYYKRIAHKQLNERGSRSALKGDASKGTYKKN GTPSNLKEICEITAKHSNDSRRDGEPCTGKDGGQVRVRTKIGTPWTKIVEINKTSYKEVF LPPRRQHMCTSNLEHLNTGNKGLKDGKLAIHSLLGDVLLAAKEQANFIKNKYKRQKASNG FKDKGTICRAIRYSYADLGDIIKGTDLWEANPGEKNTQRRLKTVFGIIKKNMPGIKDNQK YKDDEKNNPPYKLLREDWWEANRDQVWQAMKCAMKNGITCGSSDHTPLDDYIPQKLRWLT EWAEWYCKAQSKEYEKLKEKCKECKGNDQCTQDTPDCEKCKAACKKYGKNIKTWEDQWKV ISSKYKELYKQAEIYAGNGGPGYYNTKVQEEDKPVVDFLYNLYLQNGGKKGPPPDTHPSK SVTAPLKQVATVDTPSTVYSTPEGYIHQEAAMDCKQQHVFCDDNSGGKDDNKQYAFRHQP HDYDEALRCDQRDKPPPESKKVEKAKKEKDENDDGGSHHHHHHGGGSAHIVVDAYKPTK
>8C44_2 Endothelial protein C receptor (chains C) QRLHMLQISYFRDPYHVWYQGNASLGGHLTHVLEGPDTNTTIIQLQPLQEPESWARTQSG LQSYLLQFHGLVRLVHQERTLAFPLTIRCFLGCELPPEGSRAHVFFEVAVNGSSFVSFRP ERALWQADTQVTSGVVTFTLQQLNAYNRTRYELREFLEDTCVQYVQKH
| ID | Name | Formula | Copies |
|---|---|---|---|
| PTY | Phosphatidylethanolamine | C40 H80 N O8 P | 1 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
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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