9VJJ: Human Latent TGF-beta1

Crystal Structure of human Latent TGF-beta1 in complex with SOF10. Determined by X-ray diffraction at 2.48 Å resolution. Released 4 Feb 2026.

Method: X-ray diffraction
Resolution: 2.48 Å
Organism: Homo sapiens
Chains: 6
Atoms: 8,418
Mol. weight: 181.87 kDa
Released: 4 Feb 2026

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

Secondary structure: helices and β-sheets

9VJJ contains 37 α-helices and 88 β-strands across 6 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: 12 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	38-56	19
α-helix	68-69	2
α-helix	73-74	2
α-helix	75-85	11
β-strand	89	1	1
α-helix	101-103	3
β-strand	106-112	7	2
α-helix	113-115	3
α-helix	119-121	3
β-strand	131-136	6	3
α-helix	137-143	7
β-strand	150-159	10	2
β-strand	162	1	4
β-strand	166-174	9	3
β-strand	178-187	10	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	248	1	2
β-strand	257-262	6	2
α-helix	265-268	4
β-strand	295-296	2	5
β-strand	300-301	2	6
α-helix	302-306	5
β-strand	311-313	3	1
β-strand	316-317	2	6
β-strand	321-322	2	5
α-helix	343-346	4
β-strand	356-370	15	1
β-strand	373-389	17	1

Chain B: 14 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	39-56	18
α-helix	75-85	11
β-strand	89	1	2
α-helix	93-97	5
α-helix	101-103	3
β-strand	106-112	7	1
α-helix	113-115	3
β-strand	130-136	7	7
α-helix	137-143	7
α-helix	147-149	3
β-strand	150-159	10	1
β-strand	162	1	8
β-strand	166-174	9	7
β-strand	178-187	10	7
β-strand	190	1	8
β-strand	194-199	6	1
α-helix	201-210	10
β-strand	214-221	8	7
α-helix	222	1
β-strand	248	1	1
β-strand	257-262	6	1
α-helix	265-267	3
β-strand	281	1	9
α-helix	282-288	7
β-strand	294-296	3	10
α-helix	297	1
β-strand	299-301	3	11
α-helix	302-306	5
β-strand	311-313	3	2
β-strand	316-318	3	11
β-strand	321-323	3	10
α-helix	343-346	4
β-strand	356-358	3	12
β-strand	361-370	10	2
β-strand	373-384	12	2
β-strand	386	1	9
β-strand	387-389	3	12

Chain H: 4 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	13
β-strand	11-12	2	14
β-strand	18-25	8	13
α-helix	29-31	3
β-strand	34-39	6	15
β-strand	46-51	6	15
β-strand	57-59	3	15
β-strand	67-72	6	13
α-helix	73-75	3
β-strand	77-82	6	13
α-helix	87-89	3
β-strand	91-98	8	15
α-helix	105-107	3
β-strand	109-112	4	15
β-strand	116-118	3	15
β-strand	119-120	2	14

Chain I: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	16
β-strand	11-12	2	17
β-strand	18-25	8	16
α-helix	29-31	3
β-strand	34-39	6	18
β-strand	46-51	6	18
β-strand	57-59	3	18
β-strand	67-72	6	16
β-strand	77-82	6	16
α-helix	87-89	3
β-strand	91-98	8	18
α-helix	105-107	3
β-strand	109-112	4	18
β-strand	116-118	3	18
β-strand	119-120	2	17

Chain L: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	19
β-strand	10-12	3	20
β-strand	19-25	7	19
β-strand	33-38	6	20
β-strand	45-49	5	20
β-strand	53-54	2	20
β-strand	62-67	6	19
β-strand	70-75	6	19
α-helix	80-82	3
β-strand	85-91	7	20
α-helix	94-96	3
β-strand	97-99	3	20
β-strand	103-106	4	20

Chain M: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	21
β-strand	10-12	3	22
β-strand	19-25	7	21
β-strand	33-38	6	22
β-strand	45-49	5	22
β-strand	53-54	2	22
α-helix	55	1
β-strand	62-66	5	21
β-strand	70-75	6	21
β-strand	85-90	6	22
α-helix	94-96	3
β-strand	99	1	22
β-strand	103-106	4	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transforming growth factor beta-1 proprotein	A, B	protein	369	Homo sapiens	P01137 (AlphaFold model)
SOF10 Fab heavy chain	H, I	protein	227	Homo sapiens
SOF10 Fab light chain	L, M	protein	215	Homo sapiens

Sequence of entity 1 (A, B), FASTA

>9VJJ_1 Transforming growth factor beta-1 proprotein (chains A, B)
DYKDDDDKLSTSKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALY
NSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELR
EAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVT
GVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLM
ATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANF
CLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSN
MIVRSCKCS

Sequence of entity 2 (H, I), FASTA

>9VJJ_2 SOF10 Fab heavy chain (chains H, I)
QVQLVESGGGVVQPGRSLRLSCAASGFTFSSEAMNWIRQPPGKGLEWIGYIYTSGTTYRA
NWARGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGTGIYDYYYWVMDLWGPGTLVTV
SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDK

Sequence of entity 3 (L, M), FASTA

>9VJJ_3 SOF10 Fab light chain (chains L, M)
DIQMTQSPSSLSASVGDRVTITCQASQSISTYLAWYQQKPGQPPKLLIYAASTLESGVPS
RFSGSGSGTDFTLTISSLQPEDFATYYCQSYSDGDSVGFGQGTKVEIKRTVAAPSVFIFP
PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Primary citation

Selective blockade of latent TGF-beta 1 activation suppresses tissue fibrosis with good safety. Kanamori, M., Sato, I., Koo, C.X. et al. Commun Med (Lond) (2026) 6. DOI 10.1038/s43856-026-01408-w · PubMed

Other PDB entries of the same protein (UniProt P01137 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8UDZ 2.21 Å, The Structure of LTBP-49247 Fab Bound to TGFbeta1 Small Latent Complex
8C7H 2.7 Å, Cryo-EM Map of the latTGF-beta LHG-10 Fab complex
13FJ 2.75 Å, TGFB1 in complex with NIS793 FAB
6OM2 2.77 Å, Crystal structure of atypical integrin alphaV beta8 with proTGF-beta1 ligand peptide
5VQP 2.9 Å, Crystal structure of human pro-TGF-beta1
8REW 2.98 Å, CryoEM structure of human GARP-lTGFbeta1 in complex with a Fab fragment derived from an…
3KFD 3.0 Å, Ternary complex of TGF-b1 reveals isoform-specific ligand recognition and receptor…
4KV5 3.0 Å, scFv GC1009 in complex with TGF-beta1.
8VSC 3.0 Å, L-tgf-b1/GARP
9R3S 3.06 Å, pro-TGF-beta1 in complex with the third TB Domain from Latent Transforming Growth…
6GFF 3.1 Å, Structure of GARP (LRRC32) in complex with latent TGF-beta1 and MHG-8 Fab
8VSD 3.2 Å, avb8/L-TGF-b1/GARP

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