Atomic structure of the Apaf-1 apoptosome. Determined by electron microscopy at 3.8 Å resolution. Released 18 Nov 2015.
Explore 3JBT in 3D Show helices and sheets RCSB PDB PDBe
3JBT contains 280 α-helices and 539 β-strands across 14 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 |
|---|---|---|---|
| α-helix | 108-117 | 10 | |
| α-helix | 119-123 | 5 | |
| α-helix | 130-142 | 13 | |
| β-strand | 149-153 | 5 | 1 |
| α-helix | 160-169 | 10 | |
| α-helix | 171-177 | 7 | |
| β-strand | 182-188 | 7 | 1 |
| α-helix | 192-206 | 15 | |
| α-helix | 220-229 | 10 | |
| α-helix | 230-234 | 5 | |
| β-strand | 239-244 | 6 | 1 |
| α-helix | 248-254 | 7 | |
| β-strand | 260-264 | 5 | 1 |
| β-strand | 277-281 | 5 | 1 |
| α-helix | 288-299 | 12 | |
| α-helix | 308-317 | 10 | |
| α-helix | 321-333 | 13 | |
| α-helix | 338-347 | 10 | |
| α-helix | 364-373 | 10 | |
| α-helix | 377-385 | 9 | |
| β-strand | 395-396 | 2 | 2 |
| α-helix | 397-404 | 8 | |
| α-helix | 408-420 | 13 | |
| β-strand | 425 | 1 | 3 |
| β-strand | 428 | 1 | 4 |
| β-strand | 433 | 1 | 4 |
| β-strand | 434-435 | 2 | 2 |
| β-strand | 436 | 1 | 3 |
| α-helix | 439-466 | 28 | |
| α-helix | 480-494 | 15 | |
| α-helix | 497-503 | 7 | |
| α-helix | 507-516 | 10 | |
| α-helix | 521-532 | 12 | |
| α-helix | 535-549 | 15 | |
| α-helix | 551-554 | 4 | |
| α-helix | 563-566 | 4 | |
| α-helix | 576-590 | 15 | |
| α-helix | 594-596 | 3 | |
| β-strand | 597 | 1 | 5 |
| α-helix | 600-602 | 3 | |
| β-strand | 609-611 | 3 | 6 |
| α-helix | 617-618 | 2 | |
| β-strand | 621-623 | 3 | 7 |
| β-strand | 630-632 | 3 | 7 |
| β-strand | 640-643 | 4 | 7 |
| β-strand | 648-652 | 5 | 7 |
| β-strand | 660-665 | 6 | 8 |
| β-strand | 671-676 | 6 | 8 |
| β-strand | 681-685 | 5 | 8 |
| β-strand | 691-695 | 5 | 8 |
| β-strand | 702-707 | 6 | 9 |
| β-strand | 715-720 | 6 | 9 |
| β-strand | 725-729 | 5 | 9 |
| β-strand | 735-739 | 5 | 9 |
| β-strand | 746-749 | 4 | 10 |
| β-strand | 757-762 | 6 | 10 |
| β-strand | 768-771 | 4 | 10 |
| β-strand | 776-779 | 4 | 10 |
| β-strand | 804-806 | 3 | 11 |
| β-strand | 813-817 | 5 | 11 |
| β-strand | 820-825 | 6 | 11 |
| β-strand | 830-833 | 4 | 11 |
| β-strand | 836 | 1 | 11 |
| α-helix | 837 | 1 | |
| β-strand | 848 | 1 | 12 |
| α-helix | 851-853 | 3 | |
| β-strand | 854-858 | 5 | 12 |
| β-strand | 864-868 | 5 | 12 |
| β-strand | 873-876 | 4 | 12 |
| β-strand | 885-890 | 6 | 6 |
| β-strand | 896-901 | 6 | 6 |
| β-strand | 906-910 | 5 | 6 |
| α-helix | 911-915 | 5 | |
| β-strand | 928-930 | 3 | 13 |
| β-strand | 935-937 | 3 | 13 |
| β-strand | 946-947 | 2 | 14 |
| β-strand | 949-950 | 2 | 13 |
| β-strand | 958-959 | 2 | 14 |
| β-strand | 967-969 | 3 | 15 |
| α-helix | 970 | 1 | |
| β-strand | 975 | 1 | 16 |
| β-strand | 976-978 | 3 | 15 |
| β-strand | 985-986 | 2 | 15 |
| β-strand | 989 | 1 | 16 |
| β-strand | 998-999 | 2 | 15 |
| β-strand | 1009-1011 | 3 | 17 |
| β-strand | 1018-1020 | 3 | 17 |
| β-strand | 1027-1031 | 5 | 17 |
| β-strand | 1036-1040 | 5 | 17 |
| β-strand | 1049-1052 | 4 | 18 |
| β-strand | 1057-1061 | 5 | 18 |
| β-strand | 1067-1071 | 5 | 18 |
| β-strand | 1079-1081 | 3 | 18 |
| β-strand | 1090-1093 | 4 | 19 |
| β-strand | 1101-1104 | 4 | 19 |
| β-strand | 1109-1112 | 4 | 19 |
| β-strand | 1121-1123 | 3 | 19 |
| β-strand | 1132-1135 | 4 | 20 |
| β-strand | 1142-1145 | 4 | 20 |
| β-strand | 1151 | 1 | 20 |
| α-helix | 1162-1164 | 3 | |
| β-strand | 1182-1185 | 4 | 21 |
| β-strand | 1191-1195 | 5 | 21 |
| β-strand | 1199-1203 | 5 | 21 |
| β-strand | 1220 | 1 | 22 |
| β-strand | 1233-1235 | 3 | 23 |
| β-strand | 1236 | 1 | 22 |
| β-strand | 1241-1243 | 3 | 23 |
| β-strand | 1244 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-13 | 11 | |
| α-helix | 24-26 | 3 | |
| β-strand | 39 | 1 | 24 |
| α-helix | 50-54 | 5 | |
| β-strand | 58 | 1 | 24 |
| α-helix | 61-69 | 9 | |
| α-helix | 71-74 | 4 | |
| α-helix | 88-101 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptotic protease-activating factor 1 | A, C, E, G, I, K, M | protein | 1260 | Homo sapiens | O14727 (AlphaFold model) |
| Cytochrome c | B, D, F, H, J, L, N | protein | 105 | Equus caballus | P00004 (AlphaFold model) |
>3JBT_1 Apoptotic protease-activating factor 1 (chains A, C, E, G, I, K, M) MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI LKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGITSYVRTVLCEGGVP QRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPG GVHWVSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLL ILDDVWDSWVLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVN MKKADLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSYD YEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVN KSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQFQRYHQPHTLSPDQEDC MYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAV SENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINK KNITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEV LCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTNSSHHLLLATGS SDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKS INVKQFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHH STIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTS SDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLT EAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLIS SSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKVWNIITGNKEKD FVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDST LLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIK WWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLELEHHHHHHHHHH
>3JBT_2 Cytochrome c (chains B, D, F, H, J, L, N) MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITW KEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
| ID | Name | Formula | Copies |
|---|---|---|---|
| DTP | 2'-deoxyadenosine 5'-triphosphate | C10 H16 N5 O12 P3 | 7 |
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 7 |
| MG | Magnesium ion | Mg | 7 |
Atomic structure of the apoptosome: mechanism of cytochrome c- and dATP-mediated activation of Apaf-1. Zhou, M., Li, Y., Hu, Q. et al. Genes Dev (2015) 29:2349-2361. DOI 10.1101/gad.272278.115 · PubMed
Other PDB entries of the same protein (UniProt O14727 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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