Human L-TGF-beta1 in complex with the anchor protein LRRC33. Determined by electron microscopy at 4.01 Å resolution. Released 31 Aug 2022.
Explore 7Y1R in 3D Show helices and sheets RCSB PDB PDBe
7Y1R contains 28 α-helices and 63 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 |
|---|---|---|---|
| β-strand | 2 | 1 | 1 |
| α-helix | 16-28 | 13 | |
| α-helix | 43-45 | 3 | |
| α-helix | 46-56 | 11 | |
| β-strand | 77-78 | 2 | 2 |
| β-strand | 80-82 | 3 | 3 |
| α-helix | 83-85 | 3 | |
| α-helix | 90-94 | 5 | |
| β-strand | 101 | 1 | 4 |
| α-helix | 108-114 | 7 | |
| β-strand | 123-126 | 4 | 3 |
| β-strand | 138-143 | 6 | 5 |
| β-strand | 151-157 | 7 | 5 |
| α-helix | 171-173 | 3 | |
| β-strand | 190 | 1 | 4 |
| β-strand | 229-232 | 4 | 3 |
| α-helix | 253-258 | 6 | |
| β-strand | 265-267 | 3 | 6 |
| β-strand | 271-272 | 2 | 7 |
| β-strand | 284 | 1 | 8 |
| β-strand | 287-288 | 2 | 7 |
| β-strand | 292-294 | 3 | 6 |
| α-helix | 297-299 | 3 | |
| α-helix | 300-303 | 4 | |
| α-helix | 308-311 | 4 | |
| α-helix | 319-322 | 4 | |
| β-strand | 327-338 | 12 | 8 |
| β-strand | 347-360 | 14 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-27 | 23 | |
| α-helix | 32-34 | 3 | |
| α-helix | 43-45 | 3 | |
| α-helix | 46-56 | 11 | |
| α-helix | 58-59 | 2 | |
| β-strand | 78-81 | 4 | 8 |
| α-helix | 91-94 | 4 | |
| β-strand | 102 | 1 | 9 |
| β-strand | 105-107 | 3 | 10 |
| α-helix | 108-114 | 7 | |
| β-strand | 123-129 | 7 | 8 |
| β-strand | 142-143 | 2 | 11 |
| β-strand | 151-152 | 2 | 11 |
| β-strand | 166-170 | 5 | 8 |
| α-helix | 172-180 | 9 | |
| β-strand | 185-187 | 3 | 10 |
| β-strand | 188-189 | 2 | 11 |
| β-strand | 190 | 1 | 9 |
| α-helix | 226-228 | 3 | |
| β-strand | 229-233 | 5 | 8 |
| α-helix | 236-238 | 3 | |
| β-strand | 265-267 | 3 | 12 |
| β-strand | 271-272 | 2 | 13 |
| β-strand | 284 | 1 | 2 |
| β-strand | 287-288 | 2 | 13 |
| β-strand | 292-294 | 3 | 12 |
| α-helix | 300-302 | 3 | |
| α-helix | 309-317 | 9 | |
| β-strand | 328-329 | 2 | 14 |
| β-strand | 332-341 | 10 | 2 |
| β-strand | 344-355 | 12 | 2 |
| β-strand | 358-359 | 2 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 37-38 | 2 | |
| β-strand | 46-47 | 2 | 15 |
| β-strand | 53 | 1 | 16 |
| β-strand | 70-71 | 2 | 15 |
| β-strand | 77 | 1 | 16 |
| α-helix | 82-85 | 4 | |
| β-strand | 93-94 | 2 | 15 |
| β-strand | 119-121 | 3 | 15 |
| α-helix | 128-134 | 7 | |
| β-strand | 144-145 | 2 | 15 |
| β-strand | 153-154 | 2 | 17 |
| β-strand | 168-169 | 2 | 15 |
| β-strand | 177-178 | 2 | 17 |
| β-strand | 189-192 | 4 | 18 |
| β-strand | 201-202 | 2 | 19 |
| β-strand | 204 | 1 | 1 |
| β-strand | 210-213 | 4 | 18 |
| β-strand | 216 | 1 | 20 |
| β-strand | 222-223 | 2 | 19 |
| β-strand | 236-238 | 3 | 18 |
| β-strand | 240 | 1 | 20 |
| β-strand | 258-260 | 3 | 18 |
| α-helix | 327-331 | 5 | |
| β-strand | 349-350 | 2 | 21 |
| β-strand | 364-366 | 3 | 22 |
| β-strand | 373-374 | 2 | 21 |
| β-strand | 388-392 | 5 | 22 |
| β-strand | 412-415 | 4 | 22 |
| β-strand | 448-450 | 3 | 22 |
| β-strand | 471-473 | 3 | 22 |
| β-strand | 497-499 | 3 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transforming growth factor beta-1 proprotein | A, B | protein | 377 | Homo sapiens | P01137 (AlphaFold model) |
| Transforming growth factor beta activator LRRC33 | E | protein | 656 | Homo sapiens | Q86YC3 (AlphaFold model) |
>7Y1R_1 Transforming growth factor beta-1 proprotein (chains A, B) MPLLLLLPLLWAGALALSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPL PEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYM FFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSP EWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGM NRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHE PKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRK PKVEQLSNMIVRSCKCS
>7Y1R_2 Transforming growth factor beta activator LRRC33 (chains E) MPLLLLLPLLWAGALAWRNRSGTATAASQGVCKLVGGAADCRGQSLASVPSSLPPHARML TLDANPLKTLWNHSLQPYPLLESLSLHSCHLERISRGAFQEQGHLRSLVLGDNCLSENYE ETAAALHALPGLRRLDLSGNALTEDMAALMLQNLSSLRSVSLAGNTIMRLDDSVFEGLER LRELDLQRNYIFEIEGGAFDGLAELRHLNLAFNNLPCIVDFGLTRLRVLNVSYNVLEWFL ATGGEAAFELETLDLSHNQLLFFPLLPQYSKLRTLLLRDNNMGFYRDLYNTSSPREMVAQ FLLVDGNVTNITTVSLWEEFSSSDLADLRFLDMSQNQFQYLPDGFLRKMPSLSHLNLHQN CLMTLHIREHEPPGALTELDLSHNQLSELHLAPGLASCLGSLRLFNLSSNQLLGVPPGLF ANARNITTLDMSHNQISLCPLPAASDRVGPPSCVDFRNMASLRSLSLEGCGLGALPDCPF QGTSLTYLDLSSNWGVLNGSLAPLQDVAPMLQVLSLRNMGLHSSFMALDFSGFGNLRDLD LSGNCLTTFPRFGGSLALETLDLRRNSLTALPQKAVSEQLSRGLRTIYLSQNPYDCCGVD GWGALQHGQTVADWAMVTCNLSSKIIRVTELPGGVPRDCKWERLDLGSNSLEVLFQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
Specificity of TGF-beta 1 signal designated by LRRC33 and integrin alpha V beta 8. Duan, Z., Lin, X., Wang, L. et al. Nat Commun (2022) 13:4988-4988. DOI 10.1038/s41467-022-32655-9 · PubMed
Other PDB entries of the same protein (UniProt P01137 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 7Y1R 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.