Model of Munc13-1 C1-C2B-MUN-C2C 2D crystal between lipid bilayers. Determined by electron microscopy at 10.0 Å resolution. Released 9 Feb 2022.
Explore 7T81 in 3D Show helices and sheets RCSB PDB PDBe
7T81 contains 1,296 α-helices and 630 β-strands across 24 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 | 16-30 | 15 | |
| α-helix | 36-39 | 4 | |
| β-strand | 41-44 | 4 | 1 |
| β-strand | 50-51 | 2 | 2 |
| β-strand | 58-59 | 2 | 2 |
| β-strand | 60 | 1 | 3 |
| β-strand | 64 | 1 | 3 |
| β-strand | 66-69 | 4 | 1 |
| β-strand | 75-76 | 2 | 1 |
| α-helix | 88-98 | 11 | |
| α-helix | 102-122 | 21 | |
| α-helix | 124-133 | 10 | |
| α-helix | 138-153 | 16 | |
| β-strand | 161-171 | 11 | 4 |
| α-helix | 173-175 | 3 | |
| β-strand | 184-190 | 7 | 5 |
| β-strand | 193-196 | 4 | 5 |
| α-helix | 197-199 | 3 | |
| β-strand | 207-216 | 10 | 4 |
| β-strand | 222-229 | 8 | 5 |
| α-helix | 234-242 | 9 | |
| β-strand | 249-256 | 8 | 5 |
| α-helix | 257-259 | 3 | |
| β-strand | 262-269 | 8 | 4 |
| α-helix | 270 | 1 | |
| β-strand | 271 | 1 | 5 |
| β-strand | 282-291 | 10 | 4 |
| β-strand | 294 | 1 | 4 |
| α-helix | 297-299 | 3 | |
| α-helix | 300-313 | 14 | |
| α-helix | 314-319 | 6 | |
| α-helix | 334-336 | 3 | |
| α-helix | 341-353 | 13 | |
| α-helix | 358-371 | 14 | |
| α-helix | 378-395 | 18 | |
| α-helix | 404-409 | 6 | |
| α-helix | 415-433 | 19 | |
| α-helix | 436-439 | 4 | |
| α-helix | 445-467 | 23 | |
| α-helix | 477-508 | 32 | |
| α-helix | 512-514 | 3 | |
| α-helix | 531-546 | 16 | |
| α-helix | 547-551 | 5 | |
| α-helix | 552-554 | 3 | |
| α-helix | 564-590 | 27 | |
| α-helix | 595-612 | 18 | |
| α-helix | 617-620 | 4 | |
| α-helix | 626-658 | 33 | |
| β-strand | 663 | 1 | 6 |
| β-strand | 671 | 1 | 6 |
| α-helix | 672-691 | 20 | |
| α-helix | 696-728 | 33 | |
| α-helix | 735-757 | 23 | |
| α-helix | 760-762 | 3 | |
| α-helix | 765-792 | 28 | |
| α-helix | 794-808 | 15 | |
| α-helix | 814-816 | 3 | |
| α-helix | 825-850 | 26 | |
| α-helix | 853-871 | 19 | |
| α-helix | 872-876 | 5 | |
| α-helix | 880-881 | 2 | |
| α-helix | 882-886 | 5 | |
| α-helix | 899-917 | 19 | |
| α-helix | 918-920 | 3 | |
| α-helix | 925-929 | 5 | |
| α-helix | 932-945 | 14 | |
| α-helix | 948-958 | 11 | |
| β-strand | 967 | 1 | 7 |
| β-strand | 972-981 | 10 | 8 |
| β-strand | 988-998 | 11 | 8 |
| β-strand | 1010-1017 | 8 | 9 |
| β-strand | 1027-1029 | 3 | 9 |
| α-helix | 1030-1032 | 3 | |
| β-strand | 1040-1048 | 9 | 8 |
| α-helix | 1055-1057 | 3 | |
| β-strand | 1059-1066 | 8 | 9 |
| β-strand | 1074-1082 | 9 | 9 |
| α-helix | 1083-1089 | 7 | |
| β-strand | 1091-1097 | 7 | 8 |
| α-helix | 1098 | 1 | |
| β-strand | 1099 | 1 | 9 |
| α-helix | 1106-1117 | 12 | |
| α-helix | 1122-1132 | 11 | |
| β-strand | 1145 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-30 | 15 | |
| α-helix | 33-35 | 3 | |
| β-strand | 41-51 | 11 | 55 |
| β-strand | 58-59 | 2 | 55 |
| β-strand | 60 | 1 | 56 |
| β-strand | 61-63 | 3 | 55 |
| β-strand | 64 | 1 | 56 |
| β-strand | 65-69 | 5 | 55 |
| β-strand | 75-77 | 3 | 55 |
| α-helix | 78-81 | 4 | |
| α-helix | 88-99 | 12 | |
| α-helix | 103-122 | 20 | |
| α-helix | 124-133 | 10 | |
| α-helix | 138-153 | 16 | |
| β-strand | 162-171 | 10 | 57 |
| α-helix | 173-175 | 3 | |
| β-strand | 184-190 | 7 | 58 |
| β-strand | 193-196 | 4 | 58 |
| β-strand | 207-215 | 9 | 57 |
| β-strand | 222-229 | 8 | 58 |
| α-helix | 234-239 | 6 | |
| β-strand | 249-256 | 8 | 58 |
| α-helix | 257-259 | 3 | |
| β-strand | 263-269 | 7 | 57 |
| β-strand | 271 | 1 | 58 |
| β-strand | 282-289 | 8 | 57 |
| α-helix | 297-299 | 3 | |
| α-helix | 300-313 | 14 | |
| α-helix | 314-319 | 6 | |
| α-helix | 332-336 | 5 | |
| α-helix | 341-353 | 13 | |
| α-helix | 358-370 | 13 | |
| α-helix | 378-394 | 17 | |
| α-helix | 404-409 | 6 | |
| α-helix | 415-434 | 20 | |
| α-helix | 436-439 | 4 | |
| α-helix | 445-467 | 23 | |
| α-helix | 474-476 | 3 | |
| α-helix | 477-498 | 22 | |
| α-helix | 500-508 | 9 | |
| α-helix | 512-514 | 3 | |
| α-helix | 520-523 | 4 | |
| α-helix | 531-546 | 16 | |
| α-helix | 547-551 | 5 | |
| α-helix | 552-554 | 3 | |
| α-helix | 564-590 | 27 | |
| α-helix | 595-608 | 14 | |
| α-helix | 609-613 | 5 | |
| α-helix | 617-620 | 4 | |
| α-helix | 627-658 | 32 | |
| α-helix | 672-689 | 18 | |
| α-helix | 696-728 | 33 | |
| α-helix | 735-757 | 23 | |
| α-helix | 760-762 | 3 | |
| α-helix | 765-808 | 44 | |
| α-helix | 814-816 | 3 | |
| α-helix | 825-850 | 26 | |
| α-helix | 853-871 | 19 | |
| α-helix | 872-876 | 5 | |
| α-helix | 882-885 | 4 | |
| α-helix | 899-917 | 19 | |
| α-helix | 918-920 | 3 | |
| α-helix | 925-929 | 5 | |
| α-helix | 932-945 | 14 | |
| α-helix | 948-958 | 11 | |
| β-strand | 972-981 | 10 | 59 |
| β-strand | 988-998 | 11 | 59 |
| β-strand | 1010-1017 | 8 | 60 |
| β-strand | 1027-1029 | 3 | 60 |
| α-helix | 1030-1032 | 3 | |
| β-strand | 1040-1048 | 9 | 59 |
| α-helix | 1055-1057 | 3 | |
| β-strand | 1059-1066 | 8 | 60 |
| β-strand | 1074-1082 | 9 | 60 |
| α-helix | 1083-1089 | 7 | |
| β-strand | 1091-1097 | 7 | 59 |
| β-strand | 1099 | 1 | 60 |
| α-helix | 1106-1117 | 12 | |
| α-helix | 1122-1131 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein unc-13 homolog A | A, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y | protein | 1154 | Rattus norvegicus | Q4KUS2 (AlphaFold model), Q62768 (AlphaFold model) |
>7T81_1 Protein unc-13 homolog A (chains A, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y) GPLGSEFMAGITSALASSTLNNEELKNHVYKKTLQALIYPISCTTPHNFEVWTATTPTYC YECEGLLWGIARQGMRCTECGVKCHEKCQDLLNADCLQRAAEKSSKHGAEDRTQNIIMVL KDRMKIRERNKPEIFELIQEVFAVTKSAHTQQMKAVKQSVLDGTSKWSAKISITVVCAQG LQAKDKTGSSDPYVTVQVGKTKKRTKTIYGNLNPVWEENFHFECHNSSDRIKVRVWDEDD DIKSRVKQRFKRESDDFLGQTIIEVRTLSGEMDVWYNLDKRTDKSAVSGAIRLHISVEIK GEEKVAPYHVQYTCLHENLFHFVTDVQNNGVVKIPDAKGDDAWKVYYDETAQEIVDEFAM RYGVESIYQAMTHFACLSSKYMCPGVPAVMSTLLANINAYYAHTTASTNVSASDRFAASN FGKERFVKLLDQLHNSLRIDLSMYRNNFPASSPERLQDLKSTVDLLTSITFFRMKVQELQ SPPRASQVVKDCVKACLNSTYEYIFNNCHELYGREYQTDPAKKGEVPPEEQGPSIKNLDF WSKLITLIVSIIEEDKNSYTPCLNQFPQELNVGKISAEVMWSLFAQDMKYAMEEHDKHRL CKSADYMNLHFKVKWLYNEYVAELPTFKDRVPEYPAWFEPFVIQWLDENEEVSRDFLHGA LERDKKDGFQQTSEHALFSCSVVDVFSQLNQSFEIIKKLECPDPQIVGHYMRRFAKTISN VLLQYADIVSKDFASYCSKEKEKVPCILMNNTQQLRVQLEKMFEAMGGKELDAEASGTLK ELQVKLNNVLDELSHVFATSFQPHIEECVRQMGDILSQVKGTGNVPASACSSVAQDADNV LQPIMDLLDSNLTLFAKICEKTVLKRVLKELWKLVMNTMERTIVLPPEFLSKLKDHMVRE EAKSLTPKQCAVVELALDTIKQYFHAGGVGLKKTFLEKSPDLQSLRYALSLYTQATDLLI KTFVQTQSAQGSGVEDPVGEVSVHVELFTHPGTGEQKVTVKVVAANDLKWQTSGIFRPFI EVNIVGPQLSDKKRKFATKSKNNSWAPKYNESFQFSLSADAGPECYELQVCVKDYCFARE DRTVGLAVLQLRELAQRGSAACWLPLGRRIHMDDTGLTVLRILSQRSNDEVAKEFVKLKS DTRSAEEGGAAPAP
Munc13 structural transitions and oligomers that may choreograph successive stages in vesicle priming for neurotransmitter release. Grushin, K., Kalyana Sundaram, R.V., Sindelar, C.V. et al. Proc Natl Acad Sci U S A (2022) 119. DOI 10.1073/pnas.2121259119 · PubMed
Other PDB entries of the same protein (UniProt Q4KUS2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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