4KXZ: Tgfb2

crystal structure of tgfb2 in complex with GC2008. Determined by X-ray diffraction at 2.83 Å resolution. Released 24 Sept 2014.

Method: X-ray diffraction
Resolution: 2.83 Å
Organism: Homo sapiens
Chains: 12
Atoms: 16,951
Mol. weight: 241.64 kDa
Ligands: PE5
Released: 24 Sept 2014

Explore 4KXZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4KXZ contains 81 α-helices and 236 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: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	1
α-helix	4-7	4
β-strand	14	1	2
β-strand	16-18	3	3
β-strand	22-23	2	4
α-helix	24-28	5
β-strand	33-35	3	5
β-strand	38-39	2	4
β-strand	43-45	3	3
β-strand	47	1	2
β-strand	54	1	1
α-helix	57-68	12
α-helix	70-72	3
β-strand	78-80	3	1
β-strand	83-92	10	5
β-strand	95-106	12	5
β-strand	108-111	4	1

Chain B: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	6
α-helix	4-7	4
β-strand	14	1	7
β-strand	16-18	3	8
β-strand	21-23	3	9
α-helix	24-28	5
β-strand	33-35	3	10
β-strand	38-40	3	9
β-strand	43-45	3	8
β-strand	47	1	7
β-strand	54	1	6
α-helix	57-68	12
α-helix	70-72	3
β-strand	78-80	3	6
β-strand	83-92	10	10
β-strand	95-106	12	10
β-strand	108-111	4	6

Chain D: 4 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	11
α-helix	4-7	4
β-strand	14	1	12
β-strand	16-18	3	13
β-strand	21-23	3	14
α-helix	24-28	5
β-strand	33-35	3	15
β-strand	38-40	3	14
β-strand	43-45	3	13
β-strand	47	1	12
β-strand	54	1	16
α-helix	57-68	12
α-helix	70-72	3
β-strand	78-80	3	16
β-strand	83-92	10	15
β-strand	95-106	12	15
β-strand	108	1	11
β-strand	109-111	3	16

Chain E: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	17
α-helix	4-7	4
β-strand	14	1	18
β-strand	16-18	3	19
β-strand	21-23	3	20
α-helix	24-28	5
β-strand	33-35	3	21
β-strand	38-40	3	20
β-strand	43-45	3	19
β-strand	47	1	18
β-strand	54	1	17
α-helix	57-68	12
α-helix	70-72	3
β-strand	78-80	3	17
β-strand	83-92	10	21
β-strand	95-106	12	21
β-strand	109-111	3	17

Chain H: 9 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	22
α-helix	7-9	3
β-strand	10-12	3	23
β-strand	18-24	7	22
α-helix	25	1
β-strand	34-40	7	23
β-strand	44-52	9	23
β-strand	57-60	4	23
α-helix	62-64	3
β-strand	68-73	6	22
β-strand	78-83	6	22
α-helix	88-90	3
β-strand	92-99	8	23
β-strand	107-110	4	23
β-strand	111	1	22
β-strand	114-118	5	23
α-helix	122-123	2
β-strand	124	1	24
β-strand	127-131	5	25
β-strand	142-152	11	25
β-strand	153	1	24
β-strand	158-161	4	26
α-helix	162-164	3
β-strand	166	1	26
β-strand	170-172	3	25
α-helix	173-175	3
β-strand	176-177	2	25
β-strand	183-192	10	25
α-helix	193-195	3
β-strand	196	1	27
β-strand	199	1	27
β-strand	201-207	7	26
α-helix	208-210	3
β-strand	212-218	7	26

Chain I: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	45
β-strand	10-13	4	46
β-strand	19-25	7	45
β-strand	34-39	6	46
β-strand	46-50	5	46
β-strand	54-55	2	46
α-helix	56	1
β-strand	63-68	6	45
β-strand	71-76	6	45
α-helix	81-83	3
β-strand	86-91	6	46
α-helix	97	1
β-strand	98-99	2	46
β-strand	103-107	5	46
α-helix	108	1
β-strand	112	1	47
α-helix	113-114	2
β-strand	115-119	5	48
α-helix	120-122	3
α-helix	123-127	5
β-strand	130-140	11	48
β-strand	141	1	47
β-strand	146-151	6	49
β-strand	154-156	3	49
β-strand	160-164	5	48
α-helix	165-168	4
β-strand	174-183	10	48
α-helix	184-188	5
β-strand	192-198	7	49
β-strand	206-211	6	49

Chain J: 7 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	28
α-helix	7-9	3
β-strand	10-12	3	29
β-strand	18-24	7	28
α-helix	26-28	3
β-strand	34-39	6	29
β-strand	45-52	8	29
β-strand	57-60	4	29
β-strand	68-73	6	28
β-strand	78-83	6	28
α-helix	88-90	3
β-strand	92-99	8	29
β-strand	107-110	4	29
β-strand	111	1	28
β-strand	114-118	5	29
β-strand	124	1	30
β-strand	127-131	5	31
β-strand	142-152	11	31
β-strand	153	1	30
β-strand	158-161	4	32
α-helix	162-164	3
β-strand	166	1	32
β-strand	170-172	3	31
α-helix	173-175	3
β-strand	176-177	2	31
β-strand	183-192	10	31
α-helix	193-195	3
β-strand	196	1	33
β-strand	199	1	33
β-strand	202-207	6	32
α-helix	208-210	3
β-strand	212-217	6	32

Chain L: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	50
β-strand	10-13	4	51
β-strand	19-25	7	50
β-strand	34-39	6	51
β-strand	46-50	5	51
β-strand	54-55	2	51
α-helix	56	1
β-strand	63-68	6	50
β-strand	71-76	6	50
α-helix	81-83	3
β-strand	85-91	7	51
α-helix	97	1
β-strand	98-99	2	51
β-strand	103-107	5	51
β-strand	112	1	52
α-helix	113-114	2
β-strand	115-119	5	53
α-helix	120-122	3
α-helix	123-127	5
β-strand	130-140	11	53
β-strand	141	1	52
β-strand	146-151	6	54
β-strand	154-156	3	54
β-strand	160-164	5	53
α-helix	165-167	3
β-strand	174-183	10	53
α-helix	184-188	5
β-strand	192-198	7	54
β-strand	206-211	6	54

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
Transforming growth factor beta-2	A, B, D, E	protein	112	Homo sapiens	P61812 (AlphaFold model)
GC1008 Heavy Chain	H, J, N, Q	protein	224	Homo sapiens
GC1008 Light Chain	I, L, M, P	protein	215	Homo sapiens

Sequence of entity 1 (A, B, D, E), FASTA

>4KXZ_1 Transforming growth factor beta-2 (chains A, B, D, E)
ALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSR
VLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS

Sequence of entity 2 (H, J, N, Q), FASTA

>4KXZ_2 GC1008 Heavy Chain (chains H, J, N, Q)
QVQLVQSGAEVKKPGSSVKVSCKASGYTFSSNVISWVRQAPGQGLEWMGGVIPIVDIANY
AQRFKGRVTITADESTSTTYMELSSLRSEDTAVYYCASTLGLVLDAMDYWGQGTLVTVSS
ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
GLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVHHHHHH

Sequence of entity 3 (I, L, M, P), FASTA

>4KXZ_3 GC1008 Light Chain (chains I, L, M, P)
ETVLTQSPGTLSLSPGERATLSCRASQSLGSSYLAWYQQKPGQAPRLLIYGASSRAPGIP
DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYADSPITFGQGTRLEIKRTVAAPSVFIFP
PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Ligands and cofactors

ID	Name	Formula	Copies
PE5	3,6,9,12,15,18,21,24-octaoxahexacosan-1-ol	C18 H38 O9	1

Water and common crystallization additives (MES) are not listed.

Primary citation

Structures of a pan-specific antagonist antibody complexed to different isoforms of TGF beta reveal structural plasticity of antibody-antigen interactions. Moulin, A., Mathieu, M., Lawrence, C. et al. Protein Sci (2014) 23:1698-1707. DOI 10.1002/pro.2548 · 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,…
6XM2 1.91 Å, The structure of the 4A11.v7 antibody in complex with human TGFb2
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
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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