5F3H: Myostatin

Structure of myostatin in complex with humanized RK35 antibody. Determined by X-ray diffraction at 2.7 Å resolution. Released 28 Sept 2016.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Mus musculus, Homo sapiens
Chains: 12
Atoms: 15,926
Mol. weight: 236.2 kDa
Released: 28 Sept 2016

Explore 5F3H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5F3H contains 67 α-helices and 220 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: 6 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	1
β-strand	11-12	2	2
β-strand	18-23	6	1
α-helix	29-31	3
β-strand	33-39	7	3
β-strand	46-51	6	3
β-strand	58-59	2	3
β-strand	68-73	6	1
β-strand	78-83	6	1
α-helix	88-90	3
β-strand	92-99	8	3
β-strand	103-106	4	3
β-strand	110-112	3	3
β-strand	113-114	2	2
α-helix	118-119	2
β-strand	120	1	4
β-strand	123-127	5	5
β-strand	138-148	11	5
β-strand	149	1	4
β-strand	154-157	4	6
β-strand	162	1	6
β-strand	166-168	3	5
α-helix	169-171	3
β-strand	172-173	2	5
β-strand	179-188	10	5
α-helix	189-191	3
β-strand	197-203	7	6
α-helix	204-206	3
β-strand	208-214	7	6

Chain B: 8 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	7
β-strand	10-13	4	8
β-strand	19-25	7	7
β-strand	33-38	6	8
β-strand	45-49	5	8
β-strand	53-54	2	8
α-helix	55	1
β-strand	62-67	6	7
β-strand	70-75	6	7
α-helix	80-82	3
β-strand	85-90	6	8
β-strand	93	1	9
α-helix	96	1
β-strand	98	1	8
β-strand	102-106	5	8
β-strand	111	1	10
β-strand	114-118	5	11
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	11
β-strand	140	1	10
β-strand	145-150	6	12
β-strand	153-154	2	12
α-helix	155	1
β-strand	159-163	5	11
α-helix	164-167	4
β-strand	173-182	10	11
α-helix	183-187	5
β-strand	191-197	7	12
β-strand	205-210	6	12

Chains C and E: 6 helices, 23 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	33-39	7	15
β-strand	45-51	7	15
β-strand	58-59	2	15
β-strand	68-73	6	13
β-strand	78-83	6	13
α-helix	88-90	3
β-strand	92-99	8	15
β-strand	103-106	4	15
β-strand	110-112	3	15
β-strand	113-114	2	14
α-helix	118-119	2
β-strand	120	1	16
β-strand	123-127	5	17
β-strand	138-148	11	17
β-strand	149	1	16
β-strand	154-157	4	18
β-strand	162	1	18
β-strand	166-168	3	17
α-helix	169-171	3
β-strand	172-173	2	17
β-strand	179-188	10	17
α-helix	189-191	3
β-strand	197-203	7	18
α-helix	204-206	3
β-strand	208-214	7	18

Chain D: 8 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	19
β-strand	10-13	4	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
α-helix	55	1
β-strand	62-66	5	19
β-strand	71-75	5	19
α-helix	80-82	3
β-strand	85-90	6	20
β-strand	93	1	21
α-helix	96	1
β-strand	98	1	20
β-strand	102-106	5	20
α-helix	107	1
β-strand	111	1	22
β-strand	114-118	5	23
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	23
β-strand	140	1	22
β-strand	145-150	6	24
β-strand	153-155	3	24
β-strand	159-163	5	23
α-helix	164-167	4
β-strand	173-182	10	23
α-helix	183-187	5
β-strand	191-197	7	24
β-strand	205-210	6	24

Chain F: 8 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	31
β-strand	10-13	4	32
β-strand	19-25	7	31
β-strand	33-38	6	32
β-strand	45-49	5	32
β-strand	53-54	2	32
α-helix	55	1
β-strand	62-67	6	31
β-strand	70-75	6	31
α-helix	80-82	3
β-strand	85-90	6	32
β-strand	93	1	33
β-strand	98	1	32
β-strand	102-106	5	32
α-helix	107	1
β-strand	111	1	34
β-strand	114-118	5	35
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	35
β-strand	140	1	34
β-strand	145-150	6	36
β-strand	153-154	2	36
α-helix	155	1
β-strand	159-163	5	35
α-helix	164-167	4
β-strand	173-182	10	35
α-helix	183-187	5
β-strand	191-197	7	36
β-strand	205-210	6	36

Chain G: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	37
β-strand	10-12	3	38
β-strand	18-25	8	37
α-helix	29-31	3
β-strand	33-39	7	38
β-strand	46-51	6	38
β-strand	58-59	2	38
β-strand	68-73	6	37
β-strand	78-83	6	37
α-helix	88-90	3
β-strand	92-99	8	38
β-strand	103-106	4	38
β-strand	110-114	5	38
α-helix	118-119	2
β-strand	120	1	39
β-strand	123-127	5	40
β-strand	140-148	9	40
β-strand	149	1	39
β-strand	154-157	4	41
β-strand	162	1	41
β-strand	166-168	3	40
α-helix	169-171	3
β-strand	172-173	2	40
β-strand	179-186	8	40
α-helix	189-191	3
β-strand	197-203	7	41
α-helix	204-206	3
β-strand	208-214	7	41

Chain H: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	42
β-strand	10-13	4	43
β-strand	19-25	7	42
β-strand	33-38	6	43
β-strand	45-49	5	43
β-strand	53-54	2	43
α-helix	55	1
β-strand	62-65	4	42
β-strand	70-75	6	42
α-helix	80-82	3
β-strand	85-90	6	43
β-strand	93	1	44
α-helix	96	1
β-strand	98	1	43
β-strand	99	1	42
β-strand	102-106	5	43
α-helix	107	1
β-strand	111	1	45
β-strand	114-118	5	46
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	46
β-strand	140	1	45
β-strand	145-150	6	47
β-strand	153-154	2	47
α-helix	155	1
β-strand	159-163	5	46
α-helix	164-167	4
β-strand	173-182	10	46
α-helix	183-187	5
β-strand	191-197	7	47
β-strand	205-210	6	47

Chains I and J: 2 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	48
β-strand	16-18	3	48
β-strand	21-23	3	49
α-helix	24-27	4
β-strand	32-34	3	21
β-strand	37-39	3	49
β-strand	42-44	3	48
α-helix	55-64	10
β-strand	69	1	50
β-strand	74-87	14	21
β-strand	93-108	16	21

2 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
humanized RK35 antibody heavy chain	A, C, E, G	protein	221	Mus musculus
humanized RK35 antibody light chain	B, D, F, H	protein	214	Mus musculus
Growth/differentiation factor 8	I, J, K, L	protein	108	Homo sapiens	O14793 (AlphaFold model)

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

>5F3H_1 humanized RK35 antibody heavy chain (chains A, C, E, G)
EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSTISSGGSYTSY
PDSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKQDYAMNYWGQGTLVTVSSASTK
GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYS
LSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDK

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

>5F3H_2 humanized RK35 antibody light chain (chains B, D, F, H)
DIQMTQSPSSLSASVGDRVTITCKASQDVSTAVAWYQQKPGKAPKLLIYSASYRYTGVPS
RFSGSGSGTDFTLTISSLNPEDFATYYCQQHYSTPWTFGGGTKVEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

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

>5F3H_3 Growth/differentiation factor 8 (chains I, J, K, L)
FGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLV
HQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS

Primary citation

Beyond CDR-grafting: Structure-guided humanization of framework and CDR regions of an anti-myostatin antibody. Apgar, J.R., Mader, M., Agostinelli, R. et al. MAbs (2016) 8:1302-1318. DOI 10.1080/19420862.2016.1215786 · PubMed

Other PDB entries of the same protein (UniProt O14793 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5F3B 1.76 Å, Structure of myostatin in complex with chimeric RK35 antibody
5NTU 2.58 Å, Crystal Structure of human Pro-myostatin Precursor at 2.6 A Resolution
6UMX 2.79 Å, Structural basis for specific inhibition of extracellular activation of pro/latent…
5NXS 4.19 Å, Crystal Structure of Human Pro-myostatin Precursor at 4.2 A Resolution with Experimental…

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