CryoEM structure of human Mediator subunit Med23. Determined by electron microscopy at 3.1 Å resolution. Released 30 Apr 2025.
Explore 9F76 in 3D Show helices and sheets RCSB PDB PDBe
9F76 contains 91 α-helices and 3 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 | 55-69 | 15 | |
| α-helix | 73-88 | 16 | |
| α-helix | 94-103 | 10 | |
| α-helix | 112-125 | 14 | |
| α-helix | 126-128 | 3 | |
| α-helix | 131-146 | 16 | |
| α-helix | 162-171 | 10 | |
| α-helix | 180-190 | 11 | |
| α-helix | 196-198 | 3 | |
| α-helix | 203-210 | 8 | |
| α-helix | 213-218 | 6 | |
| α-helix | 224-226 | 3 | |
| α-helix | 260-263 | 4 | |
| α-helix | 267-275 | 9 | |
| α-helix | 280-287 | 8 | |
| α-helix | 298-315 | 18 | |
| α-helix | 328-343 | 16 | |
| α-helix | 349-360 | 12 | |
| α-helix | 369-382 | 14 | |
| α-helix | 389-391 | 3 | |
| α-helix | 394-402 | 9 | |
| α-helix | 408-413 | 6 | |
| α-helix | 418-422 | 5 | |
| α-helix | 424-437 | 14 | |
| α-helix | 446-448 | 3 | |
| α-helix | 452-463 | 12 | |
| α-helix | 473-480 | 8 | |
| α-helix | 489-500 | 12 | |
| β-strand | 506-508 | 3 | 1 |
| β-strand | 515-517 | 3 | 1 |
| α-helix | 522-524 | 3 | |
| α-helix | 525-530 | 6 | |
| α-helix | 533-553 | 21 | |
| α-helix | 557 | 1 | |
| β-strand | 558 | 1 | 1 |
| α-helix | 559-560 | 2 | |
| α-helix | 561-570 | 10 | |
| α-helix | 574-576 | 3 | |
| α-helix | 582-583 | 2 | |
| α-helix | 584-588 | 5 | |
| α-helix | 589-595 | 7 | |
| α-helix | 600-611 | 12 | |
| α-helix | 617-632 | 16 | |
| α-helix | 639-654 | 16 | |
| α-helix | 661-665 | 5 | |
| α-helix | 666-668 | 3 | |
| α-helix | 672-674 | 3 | |
| α-helix | 681-697 | 17 | |
| α-helix | 712-722 | 11 | |
| α-helix | 729-732 | 4 | |
| α-helix | 737-744 | 8 | |
| α-helix | 747-749 | 3 | |
| α-helix | 753-769 | 17 | |
| α-helix | 773-780 | 8 | |
| α-helix | 789-799 | 11 | |
| α-helix | 805-814 | 10 | |
| α-helix | 816-835 | 20 | |
| α-helix | 841-851 | 11 | |
| α-helix | 852-856 | 5 | |
| α-helix | 862-870 | 9 | |
| α-helix | 877-891 | 15 | |
| α-helix | 895-906 | 12 | |
| α-helix | 911-913 | 3 | |
| α-helix | 917-927 | 11 | |
| α-helix | 935-940 | 6 | |
| α-helix | 949-953 | 5 | |
| α-helix | 959-962 | 4 | |
| α-helix | 964-976 | 13 | |
| α-helix | 981-991 | 11 | |
| α-helix | 992-997 | 6 | |
| α-helix | 1001-1011 | 11 | |
| α-helix | 1020-1032 | 13 | |
| α-helix | 1046-1051 | 6 | |
| α-helix | 1065-1080 | 16 | |
| α-helix | 1092-1094 | 3 | |
| α-helix | 1100-1114 | 15 | |
| α-helix | 1119-1131 | 13 | |
| α-helix | 1142-1155 | 14 | |
| α-helix | 1158-1161 | 4 | |
| α-helix | 1163-1172 | 10 | |
| α-helix | 1175-1178 | 4 | |
| α-helix | 1188-1190 | 3 | |
| α-helix | 1200-1218 | 19 | |
| α-helix | 1221-1224 | 4 | |
| α-helix | 1227-1230 | 4 | |
| α-helix | 1231-1235 | 5 | |
| α-helix | 1242-1252 | 11 | |
| α-helix | 1253-1255 | 3 | |
| α-helix | 1256-1261 | 6 | |
| α-helix | 1265-1284 | 20 | |
| α-helix | 1291-1301 | 11 | |
| α-helix | 1302-1306 | 5 | |
| α-helix | 1312-1319 | 8 | |
| α-helix | 1323-1328 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mediator of RNA polymerase II transcription subunit 23 | A | protein | 1382 | Homo sapiens | Q9ULK4 (AlphaFold model) |
>9F76_1 Mediator of RNA polymerase II transcription subunit 23 (chains A) METQLQSIFEEVVKTEVIEEAFPGMFMDTPEDEKTKLISCLGAFRQFWGGLSQESHEQCI QWIVKFIHGQHSPKRISFLYDCLAMAVETGLLPPRLVCESLINSDTLEWERTQLWALTFK LVRKIIGGVDYKGVRDLLKVILEKILTIPNTVSSAVVQQLLAAREVIAYILERNACLLPA YFAVTEIRKLYPEGKLPHWLLGNLVSDFVDTFRPTARINSICGRCSLLPVVNNSGAICNS WKLDPATLRFPLKGLLPYDKDLFEPQTALLRYVLEQPYSRDMVCNMLGLNKQHKQRCPVL EDQLVDLVVYAMERSETEEKFDDGGTSQLLWQHLSSQLIFFVLFQFASFPHMVLSLHQKL AGRGLIKGRDHLMWVLLQFISGSIQKNALADFLPVMKLFDLLYPEKEYIPVPDINKPQST HAFAMTCIWIHLNRKAQNDNSKLQIPIPHSLRLHHEFLQQSLRNKSLQMNDYKIALLCNA YSTNSECFTLPMGALVETIYGNGIMRIPLPGTNCMASGSITPLPMNLLDSLTVHAKMSLI HSIATRVIKLAHAKSSVALAPALVETYSRLLVYMEIESLGIKGFISQLLPTVFKSHAWGI LHTLLEMFSYRMHHIQPHYRVQLLSHLHTLAAVAQTNQNQLHLCVESTALRLITALGSSE VQPQFTRFLSDPKTVLSAESEELNRALILTLARATHVTDFFTGSDSIQGTWCKDILQTIM SFTPHNWASHTLSCFPGPLQAFFKQNNVPQESRFNLKKNVEEEYRKWKSMSNENDIITHF SMQGSPPLFLCLLWKMLLETDHINQIGYRVLERIGARALVAHVRTFADFLVYEFSTSAGG QQLNKCIEILNDMVWKYNIVTLDRLILCLAMRSHEGNEAQVCYFIIQLLLLKPNDFRNRV SDFVKENSPEHWLQNDWHTKHMNYHKKYPEKLYFEGLAEQVDPPVQIQSPYLPIYFGNVC LRFLPVFDIVIHRFLELLPVSKSLETLLDHLGGLYKFHDRPVTYLYNTLHYYEMHLRDRA FLKRKLVHAIIGSLKDNRPQGWCLSDTYLKCAMNAREENPWVPDDTYYCRLIGRLVDTMA GKSPGPFPNCDWRFNEFPNPAAHALHVTCVELMALAVSGKEVGNALLNVVLKSQPLVPRE NITAWMNAIGLIITALPEPYWIVLHDRIVSVISSPSLTSETEWVGYPFRLFDFTACHQSY SEMSCSYTLALAHAVWHHSSIGQLSLIPKFLTEVLLPIVKTEFQLLYVYHLVGPFLQRFQ QERTRCMIEIGVAFYDMLLNVDQCSTHLNYMDPICDFLYHMKYMFTGDSVKEQVEKIICN LKPALKLRLRFITHISKMEPAAVPPQAMNSGSPAPQSNQVPVSLPVTQDVLFQGPGHHHH HH
Structural basis of human Mediator recruitment by the phosphorylated transcription factor Elk-1. Monte, D., Lens, Z., Dewitte, F. et al. Nat Commun (2025) 16:3772-3772. DOI 10.1038/s41467-025-59014-8 · PubMed
Other PDB entries of the same protein (UniProt Q9ULK4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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