Cooperation between the intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly. Determined by electron microscopy at 3.71 Å resolution. Released 13 Apr 2022.
Explore 7O3D in 3D Show helices and sheets RCSB PDB PDBe
7O3D contains 43 α-helices and 19 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 | 324-329 | 6 | |
| α-helix | 341-359 | 19 | |
| α-helix | 367-378 | 12 | |
| α-helix | 379-383 | 5 | |
| α-helix | 388-394 | 7 | |
| α-helix | 396-399 | 4 | |
| β-strand | 400 | 1 | 1 |
| β-strand | 408 | 1 | 1 |
| α-helix | 411-433 | 23 | |
| β-strand | 604-606 | 3 | 2 |
| α-helix | 619-621 | 3 | |
| α-helix | 631-634 | 4 | |
| α-helix | 638-649 | 12 | |
| β-strand | 653-655 | 3 | 2 |
| α-helix | 701-733 | 33 | |
| α-helix | 736-738 | 3 | |
| α-helix | 747-749 | 3 | |
| β-strand | 750-754 | 5 | 3 |
| β-strand | 765-770 | 6 | 3 |
| β-strand | 776-782 | 7 | 3 |
| α-helix | 792-806 | 15 | |
| β-strand | 810-813 | 4 | 3 |
| α-helix | 819-834 | 16 | |
| β-strand | 837 | 1 | 4 |
| β-strand | 843 | 1 | 4 |
| α-helix | 844-845 | 2 | |
| β-strand | 846-848 | 3 | 3 |
| α-helix | 852-859 | 8 | |
| α-helix | 861-866 | 6 | |
| α-helix | 872-885 | 14 | |
| α-helix | 887-893 | 7 | |
| α-helix | 896-901 | 6 | |
| α-helix | 908-910 | 3 | |
| α-helix | 913-930 | 18 | |
| β-strand | 934 | 1 | 5 |
| α-helix | 935-938 | 4 | |
| α-helix | 942-945 | 4 | |
| α-helix | 946-950 | 5 | |
| α-helix | 956-969 | 14 | |
| α-helix | 978-981 | 4 | |
| α-helix | 987-993 | 7 | |
| β-strand | 998 | 1 | 5 |
| α-helix | 1015-1018 | 4 | |
| α-helix | 1023-1025 | 3 | |
| α-helix | 1026-1037 | 12 | |
| α-helix | 1041-1050 | 10 | |
| α-helix | 1054-1062 | 9 | |
| α-helix | 1066-1070 | 5 | |
| α-helix | 1075-1086 | 12 | |
| α-helix | 1091-1102 | 12 | |
| α-helix | 1110-1112 | 3 | |
| α-helix | 1118-1125 | 8 | |
| β-strand | 1137-1141 | 5 | 6 |
| β-strand | 1145 | 1 | 6 |
| β-strand | 1150-1151 | 2 | 6 |
| β-strand | 1160-1162 | 3 | 6 |
| α-helix | 1164-1166 | 3 | |
| α-helix | 1170-1172 | 3 | |
| β-strand | 1185-1194 | 10 | 6 |
| β-strand | 1199-1203 | 5 | 6 |
| α-helix | 1206-1209 | 4 | |
| α-helix | 1227-1240 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription elongation factor SPT6 | A | protein | 1160 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P23615 (AlphaFold model) |
>7O3D_1 Transcription elongation factor SPT6 (chains A) GIDPFTDIYDLEDLKKNLMTEGDMKIRKTDIPERYQELRAGITDYGNMSSEDQELERNWI AEKISVDKNFDANYDLTEFKEAIGNAIKFITKENLEVPFIYAYRRNYISSREKDGFLLTE DDLWDIVSLDIEFHSLVNKKDYVQRFYAELHIDDPIVTEYFKNQNTASIAELNSLQDIYD YLEFKYANEINEMFINHTGKTGKKHLKNSSYEKFKASPLYQAVSDIGISAEDVGENISSQ HQIHPPVDHPSSKPVEVIESILNANSGDLQVFTSNTKLAIDTVQKYYSLELSKNTKIREK VRSDFSKYYLADVVLTAKGKKEIQKGSLYEDIKYAINRTPMHFRRDPDVFLKMVEAESLN LLSVKLHMSSQAQYIEHLFQIALETTNTSDIAIEWNNFRKLAFNQAMDKIFQDISQEVKD NLTKNCQKLVAKTVRHKFMTKLDQAPFIPNVRDPKIPKILSLTCGQGRFGADAIIAVYVN RKGDFIRDYKIVDNPFDKTNPEKFEDTLDNIIQSCQPNAIGINGPNPKTQKFYKRLQEVL HKKQIVDSRGHTIPIIYVEDEVAIRYQNSERAAQEFPNKPPLVKYCIALARYMHSPLLEY ANLTSEEVRSLSIHPHQNLLSSEQLSWALETAFVDIVNLVSVEVNKATDNNYYASALKYI SGFGKRKAIDFLQSLQRLNEPLLARQQLITHNILHKTIFMNSAGFLYISWNEKRQKYEDL EHDQLDSTRIHPEDYHLATKVAADALEYDPDTIAEKEEQGTMSEFIELLREDPDRRAKLE SLNLESYAEELEKNTGLRKLNNLNTIVLELLDGFEELRNDFHPLQGDEIFQSLTGESEKT FFKGSIIPVRVERFWHNDIICTTNSEVECVVNAQRHAGAQLRRPANEIYEIGKTYPAKVI YIDYANITAEVSLLDHDVKQQYVPISYSKDPSIWDLKQELEDAEEERKLMMAEARAKRTH RVINHPYYFPFNGRQAEDYLRSKERGEFVIRQSSRGDDHLVITWKLDKDLFQHIDIQELE KENPLALGKVLIVDNQKYNDLDQIIVEYLQNKVRLLNEMTSSEKFKSGTKKDVVKFIEDY SRVNPNKSVYYFSLNHDNPGWFYLMFKINANSKLYTWNVKLTNTGYFLVNYNYPSVIQLC NGFKTLLKSNSSKNRMNNYR
Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly. Kasiliauskaite, A., Kubicek, K., Klumpler, T. et al. Nucleic Acids Res (2022) 50:5961-5973. DOI 10.1093/nar/gkac451 · PubMed
Other PDB entries of the same protein (UniProt P23615 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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