8ACT: Human beta-cardiac myosin folded-back off state

structure of the human beta-cardiac myosin folded-back off state. Determined by electron microscopy at 3.6 Å resolution. Released 7 Jun 2023.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 6
Atoms: 18,843
Mol. weight: 277.48 kDa
Ligands: ADP, PO4, MG
Released: 7 Jun 2023

Explore 8ACT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8ACT contains 123 α-helices and 68 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: 43 helices, 27 β-strands

Element	Residues	Length	Sheet
α-helix	10-15	6
α-helix	20-27	8
β-strand	36-40	5	1
β-strand	46-55	10	1
β-strand	58-63	6	1
β-strand	68-72	5	1
α-helix	74-76	3
β-strand	78	1	1
β-strand	89	1	2
α-helix	90-92	3
α-helix	98-110	13
β-strand	115-118	4	2
β-strand	121-125	5	2
α-helix	132-134	3
α-helix	136-141	6
α-helix	154-168	15
β-strand	172-177	6	2
α-helix	184-201	18
α-helix	216-231	16
β-strand	232-233	2	3
β-strand	241-242	2	3
β-strand	246-252	7	2
α-helix	253	1
β-strand	258-265	8	2
α-helix	270-273	4
β-strand	283	1	3
α-helix	284-290	7
α-helix	295-300	6
α-helix	307-309	3
α-helix	325-338	14
α-helix	343-359	17
β-strand	363-366	4	4
β-strand	373-377	5	4
α-helix	379-388	10
α-helix	392-400	9
β-strand	403-406	4	5
β-strand	409-412	4	5
α-helix	413-414	2
α-helix	417-447	31
β-strand	456-461	6	2
α-helix	462-465	4
β-strand	471	1	6
α-helix	476-490	15
α-helix	491-495	5
α-helix	496-503	8
α-helix	519-524	6
α-helix	530-537	8
α-helix	545-555	11
β-strand	563-564	2	6
α-helix	569-571	3
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	615-620	6
α-helix	647-663	17
β-strand	666-673	8	2
α-helix	686-696	11
α-helix	700-706	7
β-strand	712-713	2	7
α-helix	715-721	7
α-helix	723-725	3
α-helix	738-747	10
β-strand	757-759	3	7
β-strand	762-764	3	7
α-helix	769-824	56
α-helix	828-839	12
α-helix	842-905	64

Chain B: 42 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	4-9	6
α-helix	10-12	3
α-helix	13-16	4
α-helix	20-27	8
β-strand	37-40	4	8
β-strand	46-49	4	8
β-strand	53-55	3	9
β-strand	58-62	5	9
β-strand	63	1	8
β-strand	68-71	4	9
β-strand	77-78	2	8
α-helix	79-81	3
α-helix	82-84	3
β-strand	89	1	10
α-helix	98-110	13
β-strand	115-118	4	10
β-strand	121-125	5	10
α-helix	136-141	6
α-helix	154-168	15
β-strand	172-178	7	10
β-strand	179	1	11
α-helix	184-197	14
α-helix	217-231	15
β-strand	233	1	12
β-strand	241	1	12
β-strand	245-252	8	10
β-strand	258-266	9	10
α-helix	271-274	4
β-strand	283	1	12
α-helix	285-288	4
α-helix	289-291	3
α-helix	295-301	7
α-helix	307-309	3
β-strand	320	1	13
β-strand	323	1	13
α-helix	325-339	15
α-helix	343-360	18
β-strand	363-366	4	14
α-helix	372	1
β-strand	373-376	4	14
α-helix	378-388	11
α-helix	392-400	9
β-strand	403-404	2	15
β-strand	411-412	2	15
α-helix	417-447	31
β-strand	455-461	7	10
α-helix	462-464	3
β-strand	465	1	11
α-helix	473-490	18
α-helix	491-496	6
α-helix	497-503	7
α-helix	518-524	7
α-helix	530-539	10
α-helix	545-556	12
β-strand	563-564	2	16
α-helix	573-574	2
β-strand	577-581	5	16
β-strand	584-588	5	16
α-helix	593-598	6
α-helix	603-610	8
α-helix	615-621	7
α-helix	647-663	17
β-strand	666-673	8	10
α-helix	686-696	11
α-helix	698-707	10
β-strand	711-714	4	17
α-helix	715-722	8
α-helix	739-747	9
β-strand	762-765	4	17
α-helix	769-825	57
α-helix	828-834	7
α-helix	837-841	5
α-helix	847-897	51

Chain C: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	48-61	14
β-strand	71-72	2	18
α-helix	76-82	7
α-helix	89-94	6
α-helix	101-105	5
β-strand	108-109	2	18
α-helix	111-124	14
α-helix	130-138	9
β-strand	148-149	2	19
α-helix	150-155	6
α-helix	156-160	5
α-helix	166-172	7
β-strand	182-183	2	19
α-helix	185-194	10

Chain D: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	48-61	14
β-strand	70-72	3	20
α-helix	73-82	10
α-helix	89-95	7
α-helix	101-106	6
β-strand	108-110	3	20
α-helix	111-124	14
α-helix	130-138	9
β-strand	147-149	3	21
α-helix	150-159	10
α-helix	166-172	7
β-strand	182-184	3	21
α-helix	185-194	10

Chain E: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	29-36	8
α-helix	47-49	3
α-helix	50-55	6
α-helix	63-72	10
α-helix	80-87	8
α-helix	88-90	3
α-helix	96-106	11
α-helix	116-122	7
α-helix	123-127	5
α-helix	132-141	10
α-helix	152-159	8

Chain F: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	23-36	14
α-helix	46-56	11
α-helix	65-72	8
α-helix	79-89	11
α-helix	96-106	11
β-strand	115	1	22
α-helix	116-125	10
α-helix	132-138	7
β-strand	149	1	22
α-helix	152-161	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin-7	A, B	protein	904	Homo sapiens	P12883 (AlphaFold model)
Myosin light chain 3	C, D	protein	157	Homo sapiens	P08590 (AlphaFold model)
Myosin regulatory light chain 2, ventricular/cardiac muscle isoform	E, F	protein	144	Homo sapiens	P10916 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8ACT_1 Myosin-7 (chains A, B)
DSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAE
TEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFC
VTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGA
GKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSS
RFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLL
ITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNM
KFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIY
ATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN
EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPK
ATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLN
ETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNL
RSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY
RILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLS
RIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKS
AEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAE
ERCD

Sequence of entity 2 (C, D), FASTA

>8ACT_2 Myosin light chain 3 (chains C, D)
ASKIKIEFTPEQIEEFKEAFMLFDRTPKCEMKITYGQCGDVLRALGQNPTQAEVLRVLGK
PRQEELNTKMMDFETFLPMLQHISKNKDTGTYEDFVEGLRVFDKEGNGTVMGAELRHVLA
TLGERLTEDEVEKLMAGQEDSNGCINYEAFVKHIMSS

Sequence of entity 3 (E, F), FASTA

>8ACT_3 Myosin regulatory light chain 2, ventricular/cardiac muscle isoform (chains E, F)
MFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINF
TVFLTMFGEKLKGADPEETILNAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMF
AAFPPDVTGNLDYKNLVHIITHGE

Ligands and cofactors

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

Primary citation

Cryo-EM structure of the folded-back state of human beta-cardiac myosin. Grinzato, A., Auguin, D., Kikuti, C. et al. Nat Commun (2023) 14:3166-3166. DOI 10.1038/s41467-023-38698-w · 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

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