9GZ1: Myosin-7

Beta-cardiac myosin interacting heads motif complexed to mavacamten. Determined by electron microscopy at 3.7 Å resolution. Released 12 Mar 2025.

Method: Electron microscopy
Resolution: 3.7 Å
Organisms: Homo sapiens, Mus musculus
Chains: 6
Atoms: 19,295
Mol. weight: 344.07 kDa
Ligands: MG, ADP, PO4, XB2
Released: 12 Mar 2025

Explore 9GZ1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GZ1 contains 129 α-helices and 65 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: 42 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
α-helix	20-28	9
β-strand	36-40	5	1
β-strand	46-54	9	1
β-strand	59-63	5	1
β-strand	68-71	4	1
α-helix	73-75	3
β-strand	77-78	2	1
α-helix	79-81	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	132-134	3
α-helix	136-140	5
α-helix	151	1
α-helix	154-168	15
β-strand	172-178	7	2
β-strand	179	1	3
α-helix	184-201	18
α-helix	215-231	17
β-strand	232-233	2	4
β-strand	241-242	2	4
β-strand	244-252	9	2
β-strand	258-268	11	2
α-helix	270-274	5
α-helix	284-290	7
α-helix	295-300	6
α-helix	307-309	3
α-helix	311-314	4
α-helix	325-339	15
α-helix	343-359	17
β-strand	364-366	3	5
β-strand	373-375	3	5
α-helix	378-388	11
α-helix	392-400	9
β-strand	403-406	4	6
β-strand	409-412	4	6
α-helix	414-416	3
α-helix	417-443	27
β-strand	448	1	2
β-strand	455-460	6	2
β-strand	465	1	3
α-helix	473-490	18
α-helix	491-496	6
α-helix	497-503	7
α-helix	518-525	8
α-helix	530-537	8
α-helix	545-556	12
β-strand	563-564	2	7
β-strand	576-579	4	7
β-strand	586-589	4	7
α-helix	593-598	6
α-helix	603-610	8
α-helix	615-621	7
α-helix	647-662	16
β-strand	666-673	8	2
α-helix	686-696	11
α-helix	698-707	10
β-strand	711-714	4	8
α-helix	715-722	8
α-helix	723-725	3
α-helix	738-748	11
α-helix	753-755	3
β-strand	756-758	3	8
β-strand	762-765	4	8
α-helix	767-825	59
α-helix	830-839	10
α-helix	841-931	91

Chain B: 44 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	4-15	12
α-helix	20-26	7
β-strand	36-40	5	9
β-strand	46-55	10	9
β-strand	58-63	6	9
β-strand	68-72	5	9
α-helix	73-75	3
β-strand	77-78	2	9
α-helix	79-81	3
α-helix	82-84	3
β-strand	89	1	10
α-helix	90-92	3
α-helix	98-109	12
β-strand	115-118	4	10
β-strand	121-125	5	10
α-helix	136-142	7
α-helix	151	1
α-helix	154-168	15
β-strand	172-177	6	10
β-strand	179	1	11
α-helix	184-201	18
α-helix	215-231	17
β-strand	232-233	2	12
β-strand	241-242	2	12
β-strand	246-252	7	10
β-strand	258-265	8	10
α-helix	270-273	4
β-strand	283	1	12
α-helix	284-292	9
α-helix	295-300	6
α-helix	307-309	3
α-helix	311-314	4
α-helix	325-338	14
α-helix	343-359	17
β-strand	364-366	3	13
β-strand	373-375	3	13
α-helix	379-388	10
α-helix	392-400	9
β-strand	403-406	4	14
β-strand	409-412	4	14
α-helix	414-416	3
α-helix	417-443	27
β-strand	455-461	7	10
α-helix	462-464	3
β-strand	465	1	11
β-strand	471	1	15
α-helix	473-490	18
α-helix	491-495	5
α-helix	496-503	8
α-helix	518-525	8
α-helix	530-537	8
α-helix	545-556	12
β-strand	563-564	2	15
β-strand	576-581	6	15
β-strand	584-589	6	15
α-helix	593-598	6
α-helix	603-611	9
α-helix	615-620	6
α-helix	647-663	17
β-strand	666-673	8	10
α-helix	686-695	10
α-helix	698-707	10
β-strand	711-714	4	16
α-helix	715-722	8
α-helix	723-725	3
α-helix	738-748	11
α-helix	753-755	3
β-strand	756-758	3	16
β-strand	762-765	4	16
α-helix	769-824	56
α-helix	829-835	7
α-helix	840-845	6
α-helix	846-931	86

Chain C: 11 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	44-55	12
β-strand	64	1	17
α-helix	65-74	10
α-helix	81-88	8
α-helix	93-98	6
β-strand	100	1	17
α-helix	103-116	14
α-helix	122-129	8
α-helix	130-132	3
β-strand	139-141	3	18
α-helix	142-147	6
α-helix	148-152	5
α-helix	158-165	8
β-strand	174-176	3	18
α-helix	177-185	9

Chain D: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	23-36	14
α-helix	46-56	11
α-helix	59-62	4
α-helix	65-72	8
α-helix	79-89	11
α-helix	96-106	11
α-helix	116-126	11
α-helix	132-139	8
α-helix	144-147	4
α-helix	152-159	8

Chain E: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	42-55	14
α-helix	68-75	8
α-helix	81-88	8
α-helix	93-98	6
α-helix	103-114	12
α-helix	122-132	11
β-strand	139-141	3	19
α-helix	142-147	6
α-helix	148-152	5
α-helix	158-165	8
β-strand	174-176	3	19
α-helix	177-186	10

Chain F: 12 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	16-22	7
α-helix	27-30	4
α-helix	31-34	4
α-helix	49-56	8
α-helix	64-72	9
α-helix	80-89	10
α-helix	90-93	4
α-helix	96-106	11
β-strand	115	1	20
α-helix	116-126	11
α-helix	132-141	10
α-helix	143-145	3
β-strand	149	1	20
α-helix	152-159	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin-7	A, B	protein	1145	Homo sapiens	P12883 (AlphaFold model)
Myosin light chain 1/3, skeletal muscle isoform	C, E	protein	187	Mus musculus	P05977 (AlphaFold model)
Myosin regulatory light chain 11	D, F	protein	168	Mus musculus	P97457 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9GZ1_1 Myosin-7 (chains A, B)
GDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTA
ETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLF
CVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESG
AGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNS
SRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML
LITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGN
MKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVI
YATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFT
NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFP
KATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPL
NETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTN
LRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR
YRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERL
SRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLK
SAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADA
EERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTL
AKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLT
KAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLK
KKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELESERTARAKVEKLRSDDYK
DDDDK

Sequence of entity 2 (C, E), FASTA

>9GZ1_2 Myosin light chain 1/3, skeletal muscle isoform (chains C, E)
APKKDVKKPAAAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQEDFKEAFLLFDRTGE
CKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMMQAISNNKDQG
GYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQEDSNGCINYEAF
VKHIMSV

Sequence of entity 3 (D, F), FASTA

>9GZ1_3 Myosin regulatory light chain 11 (chains D, F)
APKKAKRRAGAEGSSNVFSMFDQTQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRLN
VKNEELDAMMKEASGPINFTVFLTMFGEKLKGADPEDVITGAFKVLDPEGKGTIKKQFLE
ELLTTQCDRFSQEEIKNMWAAFPPDVGGNVDYKNICYVITHGDAKDQE

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	4
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2
PO4	Phosphate ion	O4 P	2
XB2	Mavacamten	C15 H19 N3 O2	2

Primary citation

Mavacamten inhibits myosin activity by stabilising the myosin interacting-heads motif and stalling motor force generation. McMillan, S.N., Pitts, J.R.T., Barua, B. et al. bioRxiv (2025). DOI 10.1101/2025.02.12.637875 · PubMed

Other PDB entries of the same protein (UniProt P12883 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5CJ1 2.1 Å, Crystal structure of the coiled coil of MYH7 residues 1526 to 1571 fused to Gp7
6PF2 2.17 Å, Crystal Structure of Amino Acids 1220-1276 of Human Beta Cardiac Myosin Fused to Gp7 and…
6PFP 2.2 Å, Crystal Structure of Amino Acids 1473-1536 of Human Beta Cardiac Myosin Fused to Gp7 and…
4PA0 2.25 Å, Omecamtiv Mercarbil binding site on the Human Beta-Cardiac Myosin Motor Domain
5CHX 2.3 Å, Crystal Structure of amino acids 1590-1657 of MYH7
5CJ0 2.3 Å, Crystal Structure of Amino Acids 1631-1692 of MYH7
5WME 2.3 Å, Crystal Structure of Amino Acids 1729-1786 of Human Beta Cardiac Myosin Fused to Gp7 as…
4XA4 2.33 Å, Crystal Structure of the coiled-coil surrounding Skip 3 of MYH7
9HTF 2.48 Å, Beta-cardiac myosin Y115H mutant motor domain in the pre-powerstroke state, MgADP.VO4 form
2FXO 2.5 Å, Structure of the human beta-myosin S2 fragment
5WJ7 2.5 Å, Crystal Structure of Amino Acids 1733-1797 of Human Beta Cardiac Myosin Fused to Xrcc4
4XA3 2.55 Å, Crystal structure of the coiled-coil surrounding Skip 2 of MYH7

Browse structure collections

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