Human Rix1 sub-complex scaffold. Determined by electron microscopy at 2.7 Å resolution. Released 2 Nov 2022.
Explore 7UWF in 3D Show helices and sheets RCSB PDB PDBe
7UWF contains 64 α-helices and 64 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 6-12 | 7 | 1 |
| β-strand | 20-24 | 5 | 1 |
| β-strand | 30-34 | 5 | 1 |
| β-strand | 39-47 | 9 | 2 |
| β-strand | 51-56 | 6 | 2 |
| β-strand | 61-66 | 6 | 2 |
| β-strand | 77-78 | 2 | 2 |
| β-strand | 83-88 | 6 | 3 |
| β-strand | 94-99 | 6 | 3 |
| β-strand | 102-107 | 6 | 3 |
| β-strand | 113-117 | 5 | 3 |
| β-strand | 124-129 | 6 | 4 |
| β-strand | 135-140 | 6 | 4 |
| β-strand | 145-149 | 5 | 4 |
| α-helix | 150-154 | 5 | |
| β-strand | 166-168 | 3 | 4 |
| β-strand | 175-180 | 6 | 5 |
| β-strand | 188-193 | 6 | 5 |
| β-strand | 197-202 | 6 | 5 |
| β-strand | 208-213 | 6 | 5 |
| β-strand | 218-223 | 6 | 6 |
| β-strand | 229-234 | 6 | 6 |
| β-strand | 239-243 | 5 | 6 |
| β-strand | 264-265 | 2 | 6 |
| β-strand | 272-277 | 6 | 7 |
| β-strand | 283-288 | 6 | 7 |
| β-strand | 292-297 | 6 | 7 |
| β-strand | 302-308 | 7 | 7 |
| β-strand | 313-320 | 8 | 1 |
| α-helix | 323-326 | 4 | |
| β-strand | 397-398 | 2 | 8 |
| α-helix | 412-426 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 32-41 | 10 | |
| α-helix | 42-44 | 3 | |
| α-helix | 66-76 | 11 | |
| α-helix | 86-100 | 15 | |
| α-helix | 105-118 | 14 | |
| α-helix | 121-139 | 19 | |
| α-helix | 145-162 | 18 | |
| α-helix | 166-185 | 20 | |
| α-helix | 189-191 | 3 | |
| α-helix | 192-205 | 14 | |
| α-helix | 208-213 | 6 | |
| α-helix | 214-225 | 12 | |
| α-helix | 230-240 | 11 | |
| α-helix | 243-245 | 3 | |
| α-helix | 250-278 | 29 | |
| α-helix | 306-326 | 21 | |
| β-strand | 334-335 | 2 | 8 |
| α-helix | 338-349 | 12 | |
| α-helix | 362-387 | 26 | |
| α-helix | 388-394 | 7 | |
| α-helix | 395-408 | 14 | |
| α-helix | 425-442 | 18 | |
| α-helix | 443-445 | 3 | |
| α-helix | 452-466 | 15 | |
| α-helix | 519-536 | 18 | |
| α-helix | 542-560 | 19 | |
| α-helix | 569-571 | 3 | |
| α-helix | 573-588 | 16 | |
| β-strand | 591 | 1 | 9 |
| β-strand | 594 | 1 | 9 |
| α-helix | 598-608 | 11 | |
| α-helix | 614-631 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| WD repeat-containing protein 18 | A, B | protein | 447 | Homo sapiens | Q9BV38 (AlphaFold model) |
| Modulator of non-genomic activity of estrogen receptor | C, D | protein | 652 | Homo sapiens | Q8IZL8 (AlphaFold model) |
>7UWF_1 WD repeat-containing protein 18 (chains A, B) MAAPMEVAVCTDSAAPMWSCIVWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKN YISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAESIHLWEVSTGNLLVILSRH YQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSVLQADPSRIPAPRHVWSHHALPITDLHC GFGGPLARVATSSLDQTVKLWEVSSGELLLSVLFDVSIMAVTMDLAEHHMFCGGSEGSIF QVDLFTWPGQRERSFHPEQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQS KQCIRTVALKGPVTNAAILLAPVSMLSSDFRPSLPLPHFNKHLLGAEHGDEPRHGGLTLR LGLHQQGSEPSYLDRTEQLQAVLCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRDLF DFSTRFITRPAKLESRGPYPYDVPDYA
>7UWF_2 Modulator of non-genomic activity of estrogen receptor (chains C, D) DYKDDDDKGTMAAAVLSGPSAGSAAGVPGGTGGLSAVSSGPRLRLLLLESVSGLLQPRTG SAVAPVHPPNRSAPHLPGLMCLLRLHGSVGGAQNLSALGALVSLSNARLSSIKTRFEGLC LLSLLVGESPTELFQQHCVSWLRSIQQVLQTQDPPATMELAVAVLRDLLRYAAQLPALFR DISMNHLPGLLTSLLGLRPECEQSALEGMKACMTYFPRACGSLKGKLASFFLSRVDALSP QLQQLACECYSRLPSLGAGFSQGLKHTESWEQELHSLLASLHTLLGALYEGAETAPVQNE GPGVEMLLSSEDGDAHVLLQLRQRFSGLARCLGLMLSSEFGAPVSVPVQEILDFICRTLS VSSKNISLHGDGPLRLLLLPSIHLEALDLLSALILACGSRLLRFGILIGRLLPQVLNSWS IGRDSLSPGQERPYSTVRTKVYAILELWVQVCGASAGMLQGGASGEALLTHLLSDISPPA DALKLRSPRGSPDGSLQTGKPSAPKKLKLDVGEAMAPPSHRKGDSNANSDVCAAALRGLS RTILMCGPLIKEETHRRLHDLVLPLVMGVQQGEVLGSSPYTSSRCRRELYCLLLALLLAP SPRCPPPLACALQAFSLGQREDSLEVSSFCSEALVTCAALTHPRVPPLQPMG
Cryo-EM reveals the architecture of the PELP1-WDR18 molecular scaffold. Gordon, J., Chapus, F.L., Viverette, E.G. et al. Nat Commun (2022) 13:6783-6783. DOI 10.1038/s41467-022-34610-0 · PubMed
Other PDB entries of the same protein (UniProt Q9BV38 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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