8V52: 2A10 Fab

Crystal structure of 2A10 Fab bound to Human TGF-beta3. Determined by X-ray diffraction at 2.5 Å resolution. Released 10 Apr 2024.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 6
Atoms: 7,812
Mol. weight: 121.43 kDa
Released: 10 Apr 2024

Explore 8V52 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8V52 contains 34 α-helices and 108 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: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	302-303	2	1
α-helix	304-309	6
β-strand	316-318	3	2
β-strand	321-323	3	3
α-helix	324-328	5
β-strand	333-335	3	4
β-strand	338-340	3	3
β-strand	343-345	3	2
β-strand	354	1	1
α-helix	357-368	12
α-helix	370-372	3
β-strand	378-380	3	1
β-strand	383-392	10	4
β-strand	395-406	12	4
β-strand	408-411	4	1

Chain B: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	302-303	2	5
α-helix	304-309	6
β-strand	316-318	3	6
β-strand	321-323	3	7
β-strand	333-335	3	8
β-strand	338-340	3	7
β-strand	343-345	3	6
β-strand	354	1	5
α-helix	357-366	10
β-strand	378-380	3	5
β-strand	383-392	10	8
β-strand	395-406	12	8
β-strand	408-411	4	5

Chain C: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	9
β-strand	10-14	5	10
β-strand	19-25	7	9
β-strand	30-31	2	11
β-strand	34-35	2	11
β-strand	37-42	6	10
β-strand	49-53	5	10
β-strand	57-58	2	10
α-helix	59	1
β-strand	66-71	6	9
β-strand	74-79	6	9
α-helix	84-86	3
β-strand	88-94	7	10
α-helix	100	1
β-strand	102	1	10
β-strand	106-111	6	10
β-strand	115	1	12
α-helix	116-117	2
β-strand	118-122	5	13
α-helix	123-125	3
α-helix	126-129	4
β-strand	133-143	11	13
β-strand	144	1	12
β-strand	149-154	6	14
β-strand	157-158	2	14
β-strand	163-167	5	13
α-helix	168-171	4
β-strand	177-186	10	13
α-helix	187-191	5
β-strand	195-201	7	14
β-strand	209-214	6	14

Chain D: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	15
β-strand	11-12	2	16
β-strand	18-25	8	15
α-helix	29-31	3
β-strand	33-39	7	17
β-strand	46-51	6	17
α-helix	54-56	3
β-strand	60-62	3	17
β-strand	70-75	6	15
β-strand	80-85	6	15
α-helix	87-89	3
β-strand	91-98	8	17
β-strand	104-105	2	17
β-strand	109-111	3	17
β-strand	112-113	2	16
α-helix	116-118	3
β-strand	119	1	18
β-strand	122-126	5	19
α-helix	127-129	3
β-strand	137-147	11	19
β-strand	148	1	18
β-strand	153-156	4	20
α-helix	157-159	3
β-strand	161	1	20
β-strand	165-167	3	19
α-helix	168-170	3
β-strand	171-172	2	19
β-strand	178-187	10	19
α-helix	188-190	3
β-strand	196-202	7	20
α-helix	203-205	3
β-strand	207-213	7	20

Chain E: 6 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	21
β-strand	12-14	3	22
β-strand	19-25	7	21
β-strand	30-31	2	23
β-strand	34-35	2	23
β-strand	37-42	6	24
β-strand	49-53	5	24
β-strand	57-58	2	24
α-helix	59	1
β-strand	66-71	6	21
β-strand	74-79	6	21
α-helix	84-86	3
β-strand	88-94	7	24
α-helix	100	1
β-strand	102	1	24
β-strand	106-108	3	24
β-strand	109-111	3	22
β-strand	115	1	25
β-strand	118-122	5	26
α-helix	123-125	3
α-helix	126-129	4
β-strand	137-141	5	26
β-strand	143	1	27
β-strand	144	1	25
β-strand	164	1	26
β-strand	167	1	28
α-helix	169-171	3
β-strand	177	1	27
β-strand	179	1	28
β-strand	180-182	3	26

Chain F: 5 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	29
β-strand	18-25	8	29
α-helix	29-31	3
β-strand	33-39	7	30
β-strand	45-51	7	30
α-helix	54-56	3
β-strand	60-62	3	30
α-helix	64-66	3
β-strand	71-75	5	29
β-strand	80-85	6	29
β-strand	91-98	8	30
β-strand	105-106	2	30
β-strand	111-112	2	30
β-strand	143-145	3	31
β-strand	154-157	4	32
α-helix	158-160	3
β-strand	166-168	3	31
α-helix	169-171	3
β-strand	181-185	5	31
β-strand	198-203	6	32
β-strand	208-213	6	32

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transforming growth factor beta-3	A, B	protein	112	Homo sapiens	P10600 (AlphaFold model)
2A10 Fab Light chain	C, E	protein	218	Homo sapiens
2A10 Fab Heavy Chain	D, F	protein	227	Homo sapiens

Sequence of entity 1 (A, B), FASTA

>8V52_1 Transforming growth factor beta-3 (chains A, B)
ALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHST
VLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS

Sequence of entity 2 (C, E), FASTA

>8V52_2 2A10 Fab Light chain (chains C, E)
DIQLTQSPSSLSASVGDRVTITCRASQSVSISRFNLMHWYQQKPGKAPKLLIYRASNLAS
GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQHSRESPWTFGGGTKVEIKRTVAAPSVF
IFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
STLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 3 (D, F), FASTA

>8V52_3 2A10 Fab Heavy Chain (chains D, F)
EVQLLESGGGLVQPGGSLRLSCAASGFDFNSYGMSWVRQAPGKGLELVSDIVSKTYNYAT
YYSDSVKDRFTISRDDSKNTLYLQMNSLRAEDTAVYYCTVAPGGSFDYWGQGTLVTVSSA
STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG
LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Primary citation

Isoform-selective TGF-beta 3 inhibition for systemic sclerosis. Sun, T., Vander Heiden, J.A., Gao, X. et al. Med (2024) 5:132-147.e7. DOI 10.1016/j.medj.2023.12.011 · PubMed

Other PDB entries of the same protein (UniProt P10600 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1TGJ 2.0 Å, Human transforming growth factor-beta 3, crystallized from dioxane
1KTZ 2.15 Å, Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex…
4UM9 2.5 Å, Crystal structure of alpha V beta 6 with peptide
8VS6 2.73 Å, L-TGF-b3/avb8
8VSB 2.93 Å, L-tgf-b3/GARP
2PJY 3.0 Å, Structural basis for cooperative assembly of the TGF-beta signaling complex
9B9F 3.0 Å, Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular…
3EO1 3.1 Å, Structure of the Fab Fragment of GC-1008 in Complex with Transforming Growth Factor-Beta 3
1TGK 3.3 Å, Human transforming growth factor beta 3, crystallized from peg 4000
9FK5 4.1 Å, Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular…

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