6XM2: 4A11.v7 antibody

The structure of the 4A11.v7 antibody in complex with human TGFb2. Determined by X-ray diffraction at 1.91 Å resolution. Released 7 Jul 2021.

Method: X-ray diffraction
Resolution: 1.91 Å
Organism: Homo sapiens
Chains: 12
Atoms: 17,117
Mol. weight: 243.11 kDa
Released: 7 Jul 2021

Explore 6XM2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6XM2 contains 83 α-helices and 229 β-strands across 12 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: 11 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-13	4	2
α-helix	18	1
β-strand	19-25	7	1
α-helix	28-29	2
α-helix	30-32	3
β-strand	35-40	6	2
β-strand	47-51	5	2
β-strand	55-56	2	2
α-helix	57	1
β-strand	64-69	6	1
β-strand	72-77	6	1
α-helix	82-84	3
β-strand	86-93	8	2
β-strand	101-103	3	2
β-strand	107-111	5	2
β-strand	116	1	3
α-helix	117-118	2
β-strand	119-123	5	4
α-helix	124-126	3
α-helix	129-131	3
β-strand	134-144	11	4
β-strand	145	1	3
β-strand	150-155	6	5
β-strand	158-159	2	5
α-helix	160	1
β-strand	164-168	5	4
α-helix	169-172	4
β-strand	178-187	10	4
α-helix	188-191	4
β-strand	196-202	7	5
β-strand	210-215	6	5

Chain B: 7 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	6
β-strand	11-12	2	7
β-strand	18-25	8	6
β-strand	34-39	6	8
β-strand	46-51	6	8
β-strand	57-59	3	8
α-helix	61-63	3
β-strand	67-72	6	6
β-strand	77-82	6	6
α-helix	87-89	3
β-strand	91-98	8	8
β-strand	112-115	4	8
β-strand	119-121	3	8
β-strand	122-123	2	7
α-helix	127-128	2
β-strand	129	1	9
β-strand	132-140	9	10
β-strand	147-157	11	10
β-strand	158	1	9
β-strand	163-166	4	11
α-helix	167-169	3
β-strand	171	1	11
β-strand	175-177	3	10
α-helix	178-180	3
β-strand	181-182	2	10
β-strand	188-197	10	10
α-helix	198-200	3
β-strand	207-212	6	11
α-helix	213-215	3
β-strand	217-222	6	11

Chain C: 10 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	12
β-strand	10-13	4	13
β-strand	19-25	7	12
α-helix	28-29	2
α-helix	30-32	3
β-strand	35-40	6	13
β-strand	47-51	5	13
β-strand	55-56	2	13
α-helix	57	1
β-strand	64-69	6	12
β-strand	72-77	6	12
α-helix	82-84	3
β-strand	86-93	8	13
β-strand	101-103	3	13
β-strand	107-111	5	13
β-strand	116	1	14
α-helix	117-118	2
β-strand	119-123	5	15
α-helix	124-126	3
α-helix	127-130	4
β-strand	134-144	11	15
β-strand	145	1	14
β-strand	150-155	6	16
β-strand	158-159	2	16
α-helix	160	1
β-strand	164-168	5	15
α-helix	169-172	4
β-strand	178-187	10	15
α-helix	188-192	5
β-strand	196-202	7	16
β-strand	210-215	6	16

Chain D: 5 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	17
β-strand	11-12	2	18
β-strand	18-25	8	17
β-strand	34-39	6	19
β-strand	46-51	6	19
β-strand	57-59	3	19
α-helix	61-63	3
β-strand	67-72	6	17
β-strand	77-82	6	17
α-helix	87-89	3
β-strand	91-98	8	19
α-helix	101	1
β-strand	112-115	4	19
β-strand	119-121	3	19
β-strand	122-123	2	18
α-helix	127-128	2
β-strand	129	1	20
β-strand	132-136	5	21
β-strand	148-157	10	21
β-strand	158	1	20
β-strand	163-166	4	22
β-strand	171	1	22
β-strand	175-177	3	21
α-helix	178-180	3
β-strand	181-182	2	21
β-strand	188-196	9	21
β-strand	206-212	7	22
β-strand	217-223	7	22

Chain E: 10 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	23
β-strand	10-13	4	24
β-strand	19-25	7	23
α-helix	28-29	2
α-helix	30-32	3
β-strand	35-40	6	24
β-strand	47-51	5	24
β-strand	55-56	2	24
α-helix	57	1
β-strand	64-69	6	23
β-strand	72-77	6	23
α-helix	82-84	3
β-strand	87-93	7	24
β-strand	101-103	3	24
β-strand	107-111	5	24
β-strand	116	1	25
α-helix	117-118	2
β-strand	119-123	5	26
α-helix	124-126	3
α-helix	128-132	5
β-strand	134-144	11	26
β-strand	145	1	25
β-strand	150-155	6	27
β-strand	158-159	2	27
α-helix	160	1
β-strand	164-168	5	26
α-helix	169-172	4
β-strand	178-187	10	26
α-helix	188-193	6
β-strand	196-202	7	27
β-strand	210-215	6	27

Chain F: 8 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	28
β-strand	11-12	2	29
α-helix	17	1
β-strand	18-25	8	28
β-strand	34-40	7	30
β-strand	46-51	6	30
β-strand	55	1	31
β-strand	57-59	3	30
α-helix	61-63	3
β-strand	67-72	6	28
α-helix	73-75	3
β-strand	77-82	6	28
α-helix	87-89	3
β-strand	91-98	8	30
β-strand	112-115	4	30
β-strand	119-121	3	30
β-strand	122-123	2	29
β-strand	129	1	32
α-helix	130-131	2
β-strand	132-136	5	33
β-strand	149-157	9	33
β-strand	158	1	32
β-strand	163-166	4	34
α-helix	167-169	3
β-strand	171	1	34
β-strand	175-177	3	33
α-helix	178-180	3
β-strand	181-182	2	33
β-strand	188-195	8	33
β-strand	207-212	6	34
α-helix	213-215	3
β-strand	217-222	6	34

Chain G: 11 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	35
β-strand	10-13	4	36
β-strand	19-25	7	35
α-helix	28-29	2
α-helix	30-32	3
β-strand	35-40	6	36
β-strand	47-51	5	36
β-strand	55-56	2	36
α-helix	57	1
β-strand	64-69	6	35
β-strand	72-77	6	35
α-helix	82-84	3
β-strand	87-93	7	36
β-strand	101-103	3	36
β-strand	107-111	5	36
α-helix	112	1
β-strand	116	1	37
α-helix	117-118	2
β-strand	119-123	5	38
α-helix	124-126	3
α-helix	127-130	4
β-strand	134-144	11	38
β-strand	145	1	37
β-strand	149-155	7	39
β-strand	158-159	2	39
α-helix	160	1
β-strand	164-168	5	38
α-helix	169-172	4
β-strand	178-187	10	38
α-helix	188-192	5
β-strand	196-203	8	39
β-strand	210-215	6	39

Chain H: 7 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	40
β-strand	11-12	2	41
β-strand	18-25	8	40
β-strand	34-39	6	42
β-strand	46-51	6	42
β-strand	55	1	43
β-strand	57-59	3	42
α-helix	61-63	3
β-strand	67-72	6	40
α-helix	73-75	3
β-strand	77-82	6	40
α-helix	87-89	3
β-strand	91-98	8	42
β-strand	112-115	4	42
β-strand	119-121	3	42
β-strand	122-123	2	41
β-strand	129	1	44
β-strand	132-136	5	45
β-strand	148-157	10	45
β-strand	158	1	44
β-strand	163-166	4	46
α-helix	167-169	3
β-strand	171	1	46
β-strand	175-177	3	45
α-helix	178-180	3
β-strand	181-182	2	45
β-strand	188-196	9	45
α-helix	198-200	3
β-strand	201	1	47
β-strand	204	1	47
β-strand	207-212	6	46
α-helix	213-215	3
β-strand	217-222	6	46

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
4A11.v7 kappa light chain Fab (VL-CL) humanized	A, C, E, G	protein	219	Homo sapiens
4A11.v7 heavy chain Fab (VH-CH1) IgG1 humanized	B, D, F, H	protein	233	Homo sapiens
Transforming growth factor beta-2	I, J, K, L	protein	112	Homo sapiens	P61812 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>6XM2_1 4A11.v7 kappa light chain Fab (VL-CL) humanized (chains A, C, E, G)
EAVLTQSPGTLSLSPGERATLSCQSSQSVYNNNYLSWFQQKPGQPPRLLIYGASTLTSGV
PDRFSGSGSGTDFTLTISRLEPEDFAVYYCAGGYSGSSDKYAFGGGTKVEIKRTVAAPSV
FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 2 (B, D, F, H), FASTA

>6XM2_2 4A11.v7 heavy chain Fab (VH-CH1) IgG1 humanized (chains B, D, F, H)
EQQLQESGPGLVKPSETLSLTCTVTGFSLSSYTVNWVRQPAGKGLEWIGYISYGGSAYYA
SWANGRFTISKDSSKNQVSLKLSSVTAADTAVYFCARHMQVGGAPTGSMAAFDPWGPGTL
VTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA
VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Sequence of entity 3 (I, J, K, L), FASTA

>6XM2_3 Transforming growth factor beta-2 (chains I, J, K, L)
ALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSR
VLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS

Primary citation

TGF beta 2 and TGF beta 3 isoforms drive fibrotic disease pathogenesis. Sun, T., Huang, Z., Liang, W.C. et al. Sci Transl Med (2021) 13. DOI 10.1126/scitranslmed.abe0407 · PubMed

Other PDB entries of the same protein (UniProt P61812 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2TGI 1.8 Å, Crystal structure of transforming growth factor-BETA2: an unusual fold for the superfamily
5TX4 1.88 Å, Derivative of mouse TGF-beta2, with a deletion of residues 52-71 and K25R, R26K, L51R,…
8DC0 1.93 Å, Rat Betaglycan Zona Pellucida Domain (ZPC) in complex with mini monomer TGFb2…
1TFG 1.95 Å, An unusual feature revealed by the crystal structure at 2.2 Å resolution of human…
6I9J 2.0 Å, Human transforming growth factor beta2 in a tetragonal crystal form
8FXV 2.2 Å, Crystal structure of human proTGF-beta2 in complex with Nb18
4KXZ 2.83 Å, crystal structure of tgfb2 in complex with GC2008.
5TY4 2.9 Å, MicroED structure of a complex between monomeric TGF-b and its receptor, TbRII, at 2.9 A…
7RCO 2.9 Å, Crystal structure of human TGF-beta-2 bound to 4A11.V2 Fab
8FXS 3.15 Å, Crystal structure of human pro-TGF-beta2 in complex with Nb9

Browse structure collections

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