Selenomethionine-substituted structure of S. cerevisiae Csn12 in complex with Thp3 and Sem1. Determined by X-ray diffraction at 2.85 Å resolution. Released 7 Sept 2022.
Explore 7EWF in 3D Show helices and sheets RCSB PDB PDBe
7EWF contains 43 α-helices and 13 β-strands across 3 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 | 207 | 1 | |
| α-helix | 213-214 | 2 | |
| α-helix | 215-231 | 17 | |
| α-helix | 236-252 | 17 | |
| α-helix | 258-273 | 16 | |
| α-helix | 277-291 | 15 | |
| α-helix | 301-314 | 14 | |
| α-helix | 318-330 | 13 | |
| α-helix | 334-337 | 4 | |
| α-helix | 340-353 | 14 | |
| α-helix | 357-362 | 6 | |
| α-helix | 369-375 | 7 | |
| α-helix | 379-393 | 15 | |
| β-strand | 394 | 1 | 1 |
| β-strand | 397-398 | 2 | 2 |
| α-helix | 399-405 | 7 | |
| α-helix | 411-419 | 9 | |
| α-helix | 424-426 | 3 | |
| β-strand | 427-432 | 6 | 2 |
| β-strand | 440-445 | 6 | 2 |
| α-helix | 447-457 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-10 | 4 | |
| α-helix | 16-22 | 7 | |
| α-helix | 27-28 | 2 | |
| α-helix | 44-67 | 24 | |
| α-helix | 76-97 | 22 | |
| α-helix | 102-104 | 3 | |
| α-helix | 105-121 | 17 | |
| α-helix | 130-145 | 16 | |
| α-helix | 157-159 | 3 | |
| α-helix | 160-173 | 14 | |
| α-helix | 177-192 | 16 | |
| α-helix | 199-201 | 3 | |
| α-helix | 203-205 | 3 | |
| α-helix | 209-220 | 12 | |
| α-helix | 221-225 | 5 | |
| α-helix | 229-241 | 13 | |
| β-strand | 244 | 1 | 3 |
| β-strand | 247 | 1 | 4 |
| β-strand | 254 | 1 | 4 |
| α-helix | 257-275 | 19 | |
| β-strand | 278-279 | 2 | 5 |
| α-helix | 284-290 | 7 | |
| α-helix | 294-309 | 16 | |
| α-helix | 312-321 | 10 | |
| α-helix | 323-328 | 6 | |
| α-helix | 332-354 | 23 | |
| β-strand | 360-362 | 3 | 1 |
| α-helix | 363-365 | 3 | |
| α-helix | 379-397 | 19 | |
| β-strand | 402-405 | 4 | 1 |
| β-strand | 410-413 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 45-47 | 3 | |
| β-strand | 48 | 1 | 3 |
| β-strand | 60-61 | 2 | 5 |
| α-helix | 72-87 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein THP3 | A | protein | 289 | Saccharomyces cerevisiae S288C | Q12049 (AlphaFold model) |
| Cop9 signalosome complex subunit 12 | B | protein | 423 | Saccharomyces cerevisiae S288C | P47130 (AlphaFold model) |
| 26S proteasome complex subunit SEM1 | C | protein | 89 | Saccharomyces cerevisiae S288C | O94742 (AlphaFold model) |
>7EWF_1 Protein THP3 (chains A) GSHMKIHVVGRCQTLEKSYLRLTSEPNPDLIRPPNILQKMYCLLMDKYQSKTATYTYLCD QFKSMRQDLRVQMIENSFTIKVYQTHARIALENGDLGEFNQCQNRIMALFENPTIPKKSY SEFICYSVLYSMLTEDYPSISHLKLKLIDDGSSEILEDEHVKMIFELSDMKLVGNYHYFM KNYLKLHKFEKCLINSFLNLEKLIFLTIICKSYNQVNLDFVKSEFNFNSIEETTNFLNEQ NLTEFILNKQITDSNGKSSNIKILNTKGCRVQLIQNYMKSKKIDIKGQK
>7EWF_2 Cop9 signalosome complex subunit 12 (chains B) MDVDIGCYFEEKRYDDKLLDFIRYDVKTPKKTKYILQRPTATDEESVRLQRFYQLGVDLK LKYSKRRSLKKQGRIKNATEELLRLANEQLKLFNRIVERETNWIIYPLWVMAKQLIRLAN ESSELNKDSIEECGRTIHRSFTICLNDRNPRLNENKKIGCYMFANLEFSIYHRLSNKDMI KNLVKVLESRVNARDIPPLNKSLAMEHKSQVVLYNYYLGQYYGCLENDHERGFFHLNEAL LQCPMLYVESTGKFVLQGQMEKIMILLVPLALLTKRLYPHWDHPVIAGVITRSKRLSQVY PTLVRSVISGNLSLYEATAASHERFFLSQGLHVVITLLREVVFTRLVQRCWQWGNDRKSI MPLKILLATKQHDSSANEDEEEQLDALECRLASAIASGLLRAYLSHSNRCIVFSKKEPFP HSK
>7EWF_3 26S proteasome complex subunit SEM1 (chains C) MSTDVAAAQAQSKIDLTKKKNEEINKKSLEEDDEFEDFPIDTWANGETIKSNAVTQTNIW EENWDDVEVDDDFTNELKAELDRYKRENQ
Structural assembly of the nucleic-acid-binding Thp3-Csn12-Sem1 complex functioning in mRNA splicing. Kuang, Z., Ke, J., Hong, J. et al. Nucleic Acids Res (2022) 50:8882-8897. DOI 10.1093/nar/gkac634 · PubMed
Other PDB entries of the same protein (UniProt Q12049 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 7EWF directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.