9YRG: PDB entry 9YRG

Cryo-EM structure of human beta-cardiac myosin in the interacting-heads motif and S2-FH undocked state. Determined by electron microscopy at 3.2 Å resolution. Released 8 Apr 2026.

Method: Electron microscopy
Resolution: 3.2 Å
Organisms: Homo sapiens, Saccharomyces cerevisiae, Aequorea victoria
Chains: 6
Atoms: 19,443
Mol. weight: 381.56 kDa
Ligands: PO4, ADP
Released: 8 Apr 2026

Explore 9YRG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9YRG contains 129 α-helices and 57 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: 45 helices, 27 β-strands

Element	Residues	Length	Sheet
α-helix	5-12	8
α-helix	20-25	6
α-helix	26-28	3
β-strand	37-40	4	1
β-strand	46-53	8	1
β-strand	59-63	5	1
β-strand	68-71	4	1
β-strand	78	1	1
α-helix	79-81	3
α-helix	82-84	3
β-strand	89	1	2
α-helix	90-92	3
α-helix	98-110	13
β-strand	115-117	3	2
β-strand	122-125	4	2
α-helix	136-141	6
α-helix	147-149	3
α-helix	154-168	15
β-strand	172-177	6	2
β-strand	179	1	3
α-helix	184-200	17
α-helix	216-231	16
β-strand	232-233	2	4
β-strand	241-242	2	4
β-strand	246-252	7	2
β-strand	258-265	8	2
α-helix	270-272	3
β-strand	283	1	4
α-helix	284-289	6
α-helix	295-301	7
α-helix	307-309	3
α-helix	325-338	14
α-helix	343-359	17
β-strand	364-366	3	5
β-strand	373-375	3	5
α-helix	379-388	10
α-helix	392-400	9
α-helix	406-408	3
α-helix	417-447	31
β-strand	455-461	7	2
α-helix	463-464	2
β-strand	465	1	3
β-strand	471	1	6
α-helix	473-490	18
α-helix	491-496	6
α-helix	497-504	8
α-helix	530-539	10
α-helix	545-556	12
β-strand	563-564	2	6
α-helix	572	1
α-helix	574	1
β-strand	577-580	4	6
β-strand	585-588	4	6
α-helix	593-598	6
α-helix	603-610	8
α-helix	615-621	7
α-helix	647-661	15
α-helix	662-664	3
β-strand	666-673	8	2
α-helix	686-696	11
α-helix	698-706	9
β-strand	711-713	3	7
α-helix	715-721	7
α-helix	727-729	3
α-helix	738-748	11
β-strand	756-758	3	7
β-strand	763-765	3	7
α-helix	769-780	12
α-helix	782-824	43
α-helix	828-836	9
α-helix	837-839	3
α-helix	845-942	98

Chain B: 42 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	5-8	4
α-helix	13-16	4
α-helix	20-28	9
β-strand	37-40	4	8
β-strand	46-53	8	8
α-helix	55-57	3
β-strand	60-63	4	8
β-strand	68-70	3	8
β-strand	77-78	2	8
α-helix	79-81	3
α-helix	82-84	3
β-strand	89	1	9
α-helix	90-92	3
α-helix	98-110	13
β-strand	116-117	2	9
β-strand	122-125	4	9
α-helix	136-141	6
α-helix	151	1
α-helix	154-168	15
β-strand	172-178	7	9
α-helix	184-195	12
α-helix	216-231	16
β-strand	233	1	10
β-strand	246-252	7	9
β-strand	261-264	4	9
α-helix	271-274	4
β-strand	283	1	10
α-helix	284-290	7
α-helix	295-301	7
α-helix	325-339	15
α-helix	343-361	19
α-helix	379-388	10
α-helix	392-400	9
β-strand	404	1	11
α-helix	417-446	30
α-helix	452-453	2
β-strand	455-461	7	9
α-helix	463-465	3
β-strand	471	1	12
α-helix	473-490	18
α-helix	491-495	5
α-helix	496-504	9
α-helix	518-525	8
α-helix	530-539	10
α-helix	545-556	12
β-strand	563-564	2	12
β-strand	577-580	4	12
β-strand	585-588	4	12
α-helix	593-597	5
β-strand	602	1	11
α-helix	603-611	9
α-helix	615-619	5
α-helix	647-662	16
β-strand	666-673	8	9
α-helix	686-696	11
α-helix	698-707	10
β-strand	712-714	3	13
α-helix	715-722	8
α-helix	723-725	3
α-helix	739-748	10
β-strand	756-758	3	13
β-strand	762-765	4	13
α-helix	769-825	57
α-helix	828-832	5
α-helix	838-840	3
α-helix	843-942	100

Chain C: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	43-56	14
β-strand	64-65	2	14
α-helix	66-75	10
α-helix	82-88	7
α-helix	95-97	3
β-strand	101-102	2	14
α-helix	104-116	13
α-helix	124-131	8
β-strand	141-142	2	15
α-helix	143-152	10
α-helix	159-165	7
β-strand	175-176	2	15
α-helix	178-184	7

Chain D: 11 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	43-56	14
α-helix	63-65	3
α-helix	67-75	9
α-helix	85-88	4
α-helix	94-99	6
α-helix	105-107	3
α-helix	108-117	10
α-helix	123-133	11
β-strand	141-142	2	16
α-helix	143-152	10
α-helix	159-166	8
β-strand	175-176	2	16
α-helix	178-185	8

Chain E: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	24-37	14
α-helix	47-56	10
α-helix	59-60	2
α-helix	69-73	5
α-helix	80-88	9
α-helix	97-107	11
α-helix	117-123	7
α-helix	124-126	3
α-helix	133-139	7
α-helix	153-161	9

Chain F: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	28-30	3
α-helix	33-36	4
α-helix	48-50	3
α-helix	52-55	4
α-helix	64-73	10
α-helix	81-91	11
α-helix	97-107	11
α-helix	117-127	11
α-helix	130-132	3
α-helix	133-142	10
α-helix	144-146	3
α-helix	153-158	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin-7,General control transcription factor GCN4,Enhanced Green fluorescent protein	A, B	protein	1315	Homo sapiens, Saccharomyces cerevisiae, Aequorea victoria	P03069 (AlphaFold model), P12883 (AlphaFold model), P42212 (AlphaFold model)
Myosin light chain 1/3, skeletal muscle isoform	C, D	protein	188	Mus musculus	P05977 (AlphaFold model)
Myosin regulatory light chain 11	E, F	protein	169	Mus musculus	P97457

Sequence of entity 1 (A, B), FASTA

>9YRG_1 Myosin-7,General control transcription factor GCN4,Enhanced Green fluorescent protein (chains A, B)
MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVT
AETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGL
FCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES
GAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDN
SSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM
LLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFG
NMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV
IYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINF
TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMF
PKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDP
LNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMT
NLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ
RYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDER
LSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLL
KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLAD
AEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELT
LAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKMKQL
EDKVEELLSKNYHLENEVARLKKLVGERGSGKLGVSKGEELFTGVVPILVELDGDVNGHK
FSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKS
AMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYN
SHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSA
LSKDPNEKRDHMVLLEFVTAAGITLGMDELYKGLNDIFEAQKIEWHEDYKDDDDK

Sequence of entity 2 (C, D), FASTA

>9YRG_2 Myosin light chain 1/3, skeletal muscle isoform (chains C, D)
MAPKKDVKKPAAAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQEDFKEAFLLFDRTG
ECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMMQAISNNKDQ
GGYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQEDSNGCINYEA
FVKHIMSV

Sequence of entity 3 (E, F), FASTA

>9YRG_3 Myosin regulatory light chain 11 (chains E, F)
MAPKKAKRRAGAEGSSNVFSMFDQTQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRL
NVKNEELDAMMKEASGPINFTVFLTMFGEKLKGADPEDVITGAFKVLDPEGKGTIKKQFL
EELLTTQCDRFSQEEIKNMWAAFPPDVGGNVDYKNICYVITHGDAKDQE

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2

Primary citation

Cryo-EM reveals how cardiomyopathy therapeutic drugs modulate the myosin motors of the heart. Somavarapu, A.K., Ge, J., Yengo, C.M. et al. Sci Adv (2026) 12:eaed6472-eaed6472. DOI 10.1126/sciadv.aed6472 · PubMed

Other PDB entries of the same protein (UniProt P03069 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3AZD 0.98 Å, Crystal structure of tropomyosin N-terminal fragment at 0.98A resolution
2WQ1 1.08 Å, GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating bromide
2WQ0 1.12 Å, GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating chloride
4OWI 1.2 Å, peptide structure
2WQ3 1.22 Å, GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating chloride and nitrate
2HY6 1.25 Å, A seven-helix coiled coil
2WPZ 1.25 Å, GCN4 leucine zipper mutant with two VxxNxxx motifs coordinating chloride
6PSA 1.3 Å, PIE12 D-peptide against HIV entry (in complex with IQN17 Q577R resistance mutant)
2IPZ 1.35 Å, A Parallel Coiled-Coil Tetramer with Offset Helices
2YNY 1.35 Å, Salmonella enterica SadA 255-302 fused to GCN4 adaptors (SadAK1)
5APU 1.35 Å, Sequence IANKEDKAD inserted between GCN4 adaptors - Structure A9b black
2WQ2 1.36 Å, GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating iodide

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