pro-TGF-beta1 in complex with the third TB Domain from Latent Transforming Growth Factor-beta Binding Protein-1. Determined by electron microscopy at 3.06 Å resolution. Released 22 Jul 2026.
Explore 9R3S in 3D Show helices and sheets RCSB PDB PDBe
9R3S contains 30 α-helices and 43 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 |
|---|---|---|---|
| α-helix | 38-56 | 19 | |
| α-helix | 62-64 | 3 | |
| α-helix | 73-74 | 2 | |
| α-helix | 75-85 | 11 | |
| β-strand | 106-112 | 7 | 6 |
| α-helix | 113-115 | 3 | |
| α-helix | 120-122 | 3 | |
| β-strand | 130-136 | 7 | 8 |
| α-helix | 137-143 | 7 | |
| α-helix | 147-149 | 3 | |
| β-strand | 150-160 | 11 | 6 |
| β-strand | 167-173 | 7 | 8 |
| β-strand | 179-186 | 8 | 8 |
| α-helix | 187-189 | 3 | |
| β-strand | 194-199 | 6 | 6 |
| α-helix | 201-210 | 10 | |
| β-strand | 214-221 | 8 | 8 |
| β-strand | 235-236 | 2 | 6 |
| β-strand | 257-262 | 6 | 6 |
| β-strand | 280 | 1 | 9 |
| α-helix | 282-286 | 5 | |
| β-strand | 294-296 | 3 | 10 |
| α-helix | 297 | 1 | |
| β-strand | 299 | 1 | 11 |
| α-helix | 302-306 | 5 | |
| β-strand | 311-313 | 3 | 2 |
| β-strand | 318 | 1 | 11 |
| β-strand | 321-323 | 3 | 10 |
| α-helix | 338-340 | 3 | |
| α-helix | 354-355 | 2 | |
| β-strand | 356-358 | 3 | 9 |
| β-strand | 361-370 | 10 | 2 |
| β-strand | 373-384 | 12 | 2 |
| β-strand | 387-389 | 3 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34 | 1 | 1 |
| α-helix | 40-56 | 17 | |
| α-helix | 72-74 | 3 | |
| α-helix | 75-85 | 11 | |
| α-helix | 87-88 | 2 | |
| α-helix | 100-103 | 4 | |
| β-strand | 106-112 | 7 | 2 |
| α-helix | 113-115 | 3 | |
| β-strand | 130-136 | 7 | 3 |
| α-helix | 137-143 | 7 | |
| β-strand | 150-159 | 10 | 2 |
| β-strand | 162 | 1 | 4 |
| β-strand | 166-173 | 8 | 3 |
| β-strand | 179-187 | 9 | 3 |
| β-strand | 190 | 1 | 4 |
| β-strand | 194-199 | 6 | 2 |
| α-helix | 201-210 | 10 | |
| β-strand | 214-221 | 8 | 3 |
| β-strand | 236 | 1 | 2 |
| β-strand | 257-262 | 6 | 2 |
| α-helix | 265-268 | 4 | |
| β-strand | 290 | 1 | 1 |
| β-strand | 299-300 | 2 | 5 |
| α-helix | 302-306 | 5 | |
| β-strand | 311-313 | 3 | 6 |
| β-strand | 317-318 | 2 | 5 |
| β-strand | 328-329 | 2 | 7 |
| α-helix | 340-342 | 3 | |
| α-helix | 343-346 | 4 | |
| β-strand | 356-370 | 15 | 6 |
| β-strand | 373-389 | 17 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1347 | 1 | 12 |
| β-strand | 1348-1349 | 2 | 7 |
| β-strand | 1367 | 1 | 12 |
| α-helix | 1369-1372 | 4 | |
| β-strand | 1380-1381 | 2 | 7 |
| β-strand | 1385-1386 | 2 | 7 |
| α-helix | 1388-1391 | 4 | |
| α-helix | 1395-1400 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transforming growth factor beta-1 proprotein | A, B | protein | 369 | Homo sapiens | P01137 (AlphaFold model) |
| Latent-transforming growth factor beta-binding protein 1 | C | protein | 435 | Homo sapiens | Q14766 (AlphaFold model) |
>9R3S_1 Transforming growth factor beta-1 proprotein (chains A, B) DYKDDDDKLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALY NSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELR EAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVT GVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLM ATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANF CLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSN MIVRSCKCS
>9R3S_2 Latent-transforming growth factor beta-binding protein 1 (chains C) APLALDVDVDQPKEEKKECYYNLNDASLCDNVLAPNVTKQECCCTSGVGWGDNCEIFPCP VLGTAEFTEMCPKGKGFVPAGESSSEAGGENYKDADECLLFGQEICKNGFCLNTRPGYEC YCKQGTYYDPVKLQCFDMDECQDPSSCIDGQCVNTEGSYNCFCTHPMVLDASEKRCIRPA ESNEQIEETDVYQDLCWEHLSDEYVCSRPLVGKQTTYTECCCLYGEAWGMQCALCPLKDS DDYAQLCNIPVTGRRQPYGRDALVDFSEQYTPEADPYFIQDRFLNSFEELQAEECGILNG CENGRCVRVQEGYTCDCFDGYHLDTAKMTCVDVNECDELNNRMSLCKNAKCINTDGSYKC LCLPGYVPSDKPNYCTPLNTALNLEKDSDLTGGGGSGGGGSGGGGSAWSHPQFEKGGGSG GGSGGSAWSHPQFEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
Structural basis for the contribution of latent TGF beta binding protein to TGF beta latency and activation. Biggin, G.R., Snee, M., Xiao, Y.B. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-75834-8 · PubMed
Other PDB entries of the same protein (UniProt P01137 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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