Structure of Ytm1 bound to the C-terminal domain of Erb1 in P 65 2 2 space group. Determined by X-ray diffraction at 3.1 Å resolution. Released 28 Oct 2015.
Explore 5CXC in 3D Show helices and sheets RCSB PDB PDBe
5CXC contains 13 α-helices and 68 β-strands across 2 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 | 15-16 | 2 | 1 |
| β-strand | 17-20 | 4 | 2 |
| β-strand | 35-36 | 2 | 1 |
| α-helix | 43-50 | 8 | |
| β-strand | 63-67 | 5 | 2 |
| β-strand | 70-71 | 2 | 2 |
| α-helix | 76-82 | 7 | |
| β-strand | 91-97 | 7 | 2 |
| α-helix | 98-101 | 4 | |
| β-strand | 104-109 | 6 | 3 |
| β-strand | 114-120 | 7 | 4 |
| α-helix | 125-131 | 7 | |
| α-helix | 138-140 | 3 | |
| β-strand | 145-150 | 6 | 4 |
| β-strand | 155-159 | 5 | 4 |
| β-strand | 164-167 | 4 | 4 |
| α-helix | 168-170 | 3 | |
| α-helix | 171-173 | 3 | |
| β-strand | 180-185 | 6 | 5 |
| β-strand | 190-195 | 6 | 5 |
| β-strand | 199-207 | 9 | 5 |
| β-strand | 213-222 | 10 | 5 |
| β-strand | 228-234 | 7 | 6 |
| β-strand | 239-244 | 6 | 6 |
| β-strand | 248-253 | 6 | 6 |
| α-helix | 260-262 | 3 | |
| β-strand | 286-287 | 2 | 5 |
| β-strand | 291-294 | 4 | 6 |
| β-strand | 300-305 | 6 | 7 |
| β-strand | 312-317 | 6 | 7 |
| β-strand | 321-326 | 6 | 7 |
| β-strand | 332-337 | 6 | 7 |
| β-strand | 342-348 | 7 | 8 |
| β-strand | 357-362 | 6 | 8 |
| β-strand | 367-370 | 4 | 8 |
| β-strand | 382-384 | 3 | 8 |
| β-strand | 391-396 | 6 | 9 |
| β-strand | 403-408 | 6 | 9 |
| β-strand | 412-417 | 6 | 9 |
| β-strand | 422 | 1 | 8 |
| β-strand | 434-435 | 2 | 8 |
| β-strand | 439-442 | 4 | 9 |
| α-helix | 454-455 | 2 | |
| β-strand | 463-467 | 5 | 3 |
| β-strand | 474-477 | 4 | 3 |
| β-strand | 481-485 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 445-449 | 5 | 10 |
| β-strand | 456-461 | 6 | 11 |
| β-strand | 467-472 | 6 | 11 |
| β-strand | 476-481 | 6 | 11 |
| β-strand | 487-492 | 6 | 11 |
| β-strand | 499-504 | 6 | 12 |
| β-strand | 513-517 | 5 | 12 |
| β-strand | 520-524 | 5 | 12 |
| α-helix | 533-544 | 12 | |
| β-strand | 568-570 | 3 | 12 |
| α-helix | 575-578 | 4 | |
| β-strand | 581-586 | 6 | 12 |
| β-strand | 593-596 | 4 | 13 |
| β-strand | 602-606 | 5 | 13 |
| α-helix | 611-613 | 3 | |
| β-strand | 615-619 | 5 | 13 |
| β-strand | 624-626 | 3 | 13 |
| β-strand | 636-641 | 6 | 14 |
| β-strand | 647-652 | 6 | 14 |
| β-strand | 656-660 | 5 | 14 |
| β-strand | 665-670 | 6 | 14 |
| β-strand | 677-682 | 6 | 15 |
| β-strand | 688-693 | 6 | 15 |
| β-strand | 698-702 | 5 | 15 |
| β-strand | 711-713 | 3 | 15 |
| β-strand | 720-725 | 6 | 16 |
| β-strand | 732-737 | 6 | 16 |
| β-strand | 742-748 | 7 | 16 |
| β-strand | 758-765 | 8 | 16 |
| α-helix | 768-770 | 3 | |
| β-strand | 771 | 1 | 17 |
| β-strand | 774 | 1 | 17 |
| β-strand | 776-781 | 6 | 10 |
| β-strand | 788-792 | 5 | 10 |
| β-strand | 797-800 | 4 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribosome biogenesis protein YTM1 | A | protein | 510 | Chaetomium thermophilum | G0SFB5 (AlphaFold model) |
| Ribosome biogenesis protein ERB1 | B | protein | 369 | Chaetomium thermophilum | G0SCK6 (AlphaFold model) |
>5CXC_1 Ribosome biogenesis protein YTM1 (chains A) MAHHHHHHSSGLEVLMDAPMEDAPAPVAQVKVIFTTTEPDLELPESKRQLLVPADIRRYG LSRILNSESMLDTGSIPFDFLINGSFLRSSLEDYLTSNGLSLETTLTLQYVRSLIPPVYE ASFEHDDWVSAVDVLSATSPAGRWSSAANSSAAVQPGQERVLSASYDGLLRIWNASGSVI ATSPSGSHGGHTASIKAAKFLTSDRLASAGMDRTVRVWKYTESDHFTGELKPTLELYGHT GSVDWLDVDGHSKHILTASADGAIGFWSASKASAPEPDASLLPGAHVSKRRKATSSVSTA QRGPLGLWSIHTAPATAAIFDPRDRTVAYSASQDHTVRTLDLTTGQVVSTLTLTHPLLSL SALTRAGTTSPLLAAGTSARHITMVDPRASSATTSVMTLRGHANKVVSLSPSPENEYSLV SGSHDGTCRVWDLRSVRPATKEEGSLGGVSEPVYVIERESWASKGKKKRPVAGDGCKVFS VVWDKLGIFSGGEDKKVQVNRGRNIVTEQK
>5CXC_2 Ribosome biogenesis protein ERB1 (chains B) PSPDELKPFPTVQQTIFRGHEGRVRSVAIDPTGVALATGGDDGTVRVWELLTGRQVWSVK LNGDEAVNTVRWRPTKDTFILAAAAGEDIFLMIPTHPSVTPALDQASRDILNAGFGHATN GKQQANLPPGKEPPGKWARPGTRLEDEGVLLRITVRSTIKAISWHRRGDHFATVSPSGQR SSVAIHTLSKHLTQIPFRKLNGLAQTASFHPLRPLFFVATQRSIRCYDLQKLELVKIVQP GAKWISSFDVHPGGDNLVVGSYDKRLLWHDLDLSNRPYKTMRFHTEAIRAVRFHKGGLPL FADASDDGSLQIFHGKVPNDQLENPTIVPVKMLKGHKVVNKLGVLDIDWHPREPWCVSAG ADGTARLWM
The structure of Erb1-Ytm1 complex reveals the functional importance of a high-affinity binding between two beta-propellers during the assembly of large ribosomal subunits in eukaryotes. Wegrecki, M., Rodriguez-Galan, O., de la Cruz, J. et al. Nucleic Acids Res (2015) 43:11017-11030. DOI 10.1093/nar/gkv1043 · PubMed
Other PDB entries of the same protein (UniProt G0SFB5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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