5F3B: Myostatin

Structure of myostatin in complex with chimeric RK35 antibody. Determined by X-ray diffraction at 1.76 Å resolution. Released 28 Sept 2016.

Method: X-ray diffraction
Resolution: 1.76 Å
Organisms: Mus musculus, Homo sapiens
Chains: 6
Atoms: 9,462
Mol. weight: 119.33 kDa
Released: 28 Sept 2016

Explore 5F3B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5F3B contains 49 α-helices and 110 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: 10 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	11-12	2	2
β-strand	18-25	8	1
α-helix	29-31	3
β-strand	33-39	7	3
β-strand	45-51	7	3
β-strand	58-59	2	3
β-strand	69-73	5	1
α-helix	74-76	3
β-strand	78-83	6	1
α-helix	88-90	3
β-strand	92-99	8	3
β-strand	103-104	2	3
β-strand	110-112	3	3
β-strand	113-114	2	2
α-helix	118-119	2
β-strand	120	1	4
α-helix	121-122	2
β-strand	123-127	5	5
α-helix	128-130	3
β-strand	138-148	11	5
β-strand	149	1	4
β-strand	154-157	4	6
α-helix	158-160	3
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	198-203	6	6
α-helix	204-206	3
β-strand	208-213	6	6

Chains B and F: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	7
β-strand	10-13	4	3
β-strand	19-25	7	7
β-strand	33-38	6	3
β-strand	45-49	5	3
β-strand	53-54	2	3
α-helix	55	1
β-strand	62-67	6	7
β-strand	70-75	6	7
α-helix	80-82	3
β-strand	84-90	7	3
β-strand	93	1	8
α-helix	96	1
β-strand	97-98	2	3
β-strand	102-106	5	3
β-strand	111	1	9
α-helix	112-113	2
β-strand	114-118	5	10
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	10
β-strand	140	1	9
β-strand	145-150	6	11
β-strand	153-154	2	11
α-helix	155	1
β-strand	159-163	5	10
α-helix	164-167	4
β-strand	173-182	10	10
α-helix	183-187	5
β-strand	191-197	7	11
β-strand	205-210	6	11

Chain C: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
β-strand	5	1	23
β-strand	14	1	24
β-strand	16-18	3	23
α-helix	19	1
β-strand	21-23	3	25
α-helix	24-27	4
β-strand	32-34	3	8
β-strand	37-39	3	25
β-strand	42-44	3	23
β-strand	46	1	24
α-helix	52-54	3
α-helix	55-64	10
β-strand	69	1	26
β-strand	74-87	14	8
β-strand	93-108	16	8

Chain D: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
β-strand	5	1	26
β-strand	16-18	3	26
α-helix	19	1
β-strand	21-23	3	27
α-helix	24-27	4
β-strand	32-34	3	19
β-strand	37-39	3	27
β-strand	42-44	3	26
α-helix	52-54	3
α-helix	55-64	10
β-strand	69	1	23
β-strand	74-87	14	19
β-strand	93-108	16	19

Chain E: 11 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	12
β-strand	11-12	2	13
β-strand	18-25	8	12
α-helix	29-31	3
β-strand	33-39	7	14
β-strand	45-51	7	14
β-strand	58-59	2	14
β-strand	69-73	5	12
α-helix	74-76	3
β-strand	78-83	6	12
α-helix	88-90	3
β-strand	92-99	8	14
β-strand	103-104	2	14
β-strand	110-112	3	14
β-strand	113-114	2	13
α-helix	118-119	2
β-strand	120	1	15
α-helix	121-122	2
β-strand	123-127	5	16
α-helix	128-130	3
α-helix	133-134	2
β-strand	138-148	11	16
β-strand	149	1	15
β-strand	154-157	4	17
α-helix	158-160	3
β-strand	162	1	17
β-strand	166-168	3	16
α-helix	169-171	3
β-strand	172-173	2	16
β-strand	179-188	10	16
α-helix	189-191	3
β-strand	198-203	6	17
α-helix	204-206	3
β-strand	208-213	6	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RK35 Chimeric antibody heavy chain	A, E	protein	221	Mus musculus
RK35 Chimeric antibody light chain	B, F	protein	213	Mus musculus
Growth/differentiation factor 8	C, D	protein	109	Homo sapiens	O14793 (AlphaFold model)

Sequence of entity 1 (A, E), FASTA

>5F3B_1 RK35 Chimeric antibody heavy chain (chains A, E)
EVQLVESGGGLVKPGGSLKLSCAASGFTFSSYAMSWVRQTPEKRLEWVATISSGGSYTSY
PDSVKGRFTISRDNAKNTLYLQMSSLRSEDTAMYYCARQDYAMNYWGQGTLVTVSSASTK
GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYS
LSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDK

Sequence of entity 2 (B, F), FASTA

>5F3B_2 RK35 Chimeric antibody light chain (chains B, F)
DIEMTQSHKFMSTSVGDRVSITCKASQDVSTAVAWYQQKPGQSPKLLLYSASYRYTGVPD
RFTGSGSGTDFTFTISSVNAEDLAVYYCQQHYSTPWTFGGGTKVEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE

Sequence of entity 3 (C, D), FASTA

>5F3B_3 Growth/differentiation factor 8 (chains C, D)
DFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHL
VHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS

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:

5NTU 2.58 Å, Crystal Structure of human Pro-myostatin Precursor at 2.6 A Resolution
5F3H 2.7 Å, Structure of myostatin in complex with humanized RK35 antibody
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…

Browse structure collections

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