9R3S: Pro-TGF-beta1

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.

Method
Electron microscopy
Resolution
3.06 Å
Organism
Homo sapiens
Chains
3
Atoms
6,003
Mol. weight
135.1 kDa
Ligands
NAG
Released
22 Jul 2026

Explore 9R3S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 15 helices, 19 β-strands

ElementResiduesLengthSheet
α-helix38-5619
α-helix62-643
α-helix73-742
α-helix75-8511
β-strand106-11276
α-helix113-1153
α-helix120-1223
β-strand130-13678
α-helix137-1437
α-helix147-1493
β-strand150-160116
β-strand167-17378
β-strand179-18688
α-helix187-1893
β-strand194-19966
α-helix201-21010
β-strand214-22188
β-strand235-23626
β-strand257-26266
β-strand28019
α-helix282-2865
β-strand294-296310
α-helix2971
β-strand299111
α-helix302-3065
β-strand311-31332
β-strand318111
β-strand321-323310
α-helix338-3403
α-helix354-3552
β-strand356-35839
β-strand361-370102
β-strand373-384122
β-strand387-38939
Chain B: 12 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3411
α-helix40-5617
α-helix72-743
α-helix75-8511
α-helix87-882
α-helix100-1034
β-strand106-11272
α-helix113-1153
β-strand130-13673
α-helix137-1437
β-strand150-159102
β-strand16214
β-strand166-17383
β-strand179-18793
β-strand19014
β-strand194-19962
α-helix201-21010
β-strand214-22183
β-strand23612
β-strand257-26262
α-helix265-2684
β-strand29011
β-strand299-30025
α-helix302-3065
β-strand311-31336
β-strand317-31825
β-strand328-32927
α-helix340-3423
α-helix343-3464
β-strand356-370156
β-strand373-389176
Chain C: 3 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand1347112
β-strand1348-134927
β-strand1367112
α-helix1369-13724
β-strand1380-138127
β-strand1385-138627
α-helix1388-13914
α-helix1395-14006

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transforming growth factor beta-1 proproteinA, Bprotein369Homo sapiensP01137 (AlphaFold model)
Latent-transforming growth factor beta-binding protein 1Cprotein435Homo sapiensQ14766 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9R3S_1 Transforming growth factor beta-1 proprotein (chains A, B)
DYKDDDDKLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALY
NSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELR
EAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVT
GVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLM
ATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANF
CLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSN
MIVRSCKCS
Sequence of entity 2 (C), FASTA
>9R3S_2 Latent-transforming growth factor beta-binding protein 1 (chains C)
APLALDVDVDQPKEEKKECYYNLNDASLCDNVLAPNVTKQECCCTSGVGWGDNCEIFPCP
VLGTAEFTEMCPKGKGFVPAGESSSEAGGENYKDADECLLFGQEICKNGFCLNTRPGYEC
YCKQGTYYDPVKLQCFDMDECQDPSSCIDGQCVNTEGSYNCFCTHPMVLDASEKRCIRPA
ESNEQIEETDVYQDLCWEHLSDEYVCSRPLVGKQTTYTECCCLYGEAWGMQCALCPLKDS
DDYAQLCNIPVTGRRQPYGRDALVDFSEQYTPEADPYFIQDRFLNSFEELQAEECGILNG
CENGRCVRVQEGYTCDCFDGYHLDTAKMTCVDVNECDELNNRMSLCKNAKCINTDGSYKC
LCLPGYVPSDKPNYCTPLNTALNLEKDSDLTGGGGSGGGGSGGGGSAWSHPQFEKGGGSG
GGSGGSAWSHPQFEK

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O61

Primary citation

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:

Browse structure collections

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