8EFH: Beta-cardiac myosin II

Helical reconstruction of the human cardiac actin-tropomyosin-myosin complex in complex with ADP-Mg2+. Determined by electron microscopy at 3.3 Å resolution. Released 11 Jan 2023.

Method: Electron microscopy
Resolution: 3.3 Å
Organisms: Homo sapiens, Sus scrofa
Chains: 8
Atoms: 23,228
Mol. weight: 377.72 kDa
Ligands: ADP, MG
Released: 11 Jan 2023

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

Secondary structure: helices and β-sheets

8EFH contains 149 α-helices and 131 β-strands across 8 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: 34 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	14-16	3
α-helix	23-26	4
β-strand	36-39	4	1
β-strand	47-55	9	1
β-strand	58-63	6	1
β-strand	70-72	3	1
β-strand	77	1	1
β-strand	89	1	2
α-helix	98-110	13
β-strand	115-118	4	2
β-strand	121-125	5	2
α-helix	132-134	3
α-helix	136-142	7
α-helix	151	1
α-helix	154-167	14
β-strand	172-178	7	2
α-helix	184-196	13
α-helix	217-230	14
β-strand	232-233	2	3
β-strand	241-242	2	3
β-strand	245-252	8	2
β-strand	258-266	9	2
α-helix	270-274	5
β-strand	283	1	3
α-helix	284-289	6
α-helix	295-301	7
α-helix	307-309	3
α-helix	311-314	4
α-helix	325-337	13
α-helix	344-358	15
β-strand	365-366	2	4
α-helix	367	1
β-strand	373-374	2	4
α-helix	380-388	9
α-helix	392-400	9
β-strand	403-406	4	5
β-strand	409-412	4	5
α-helix	417-447	31
β-strand	454-463	10	2
β-strand	471	1	6
α-helix	473-504	32
α-helix	518-524	7
α-helix	530-538	9
α-helix	545-556	12
β-strand	557	1	7
β-strand	560	1	7
β-strand	563-564	2	6
β-strand	577-580	4	6
β-strand	585-588	4	6
α-helix	593-597	5
β-strand	598	1	8
α-helix	604-609	6
α-helix	616-619	4
β-strand	646	1	8
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	9
α-helix	715-721	7
α-helix	722-725	4
α-helix	739-747	9
β-strand	756-757	2	9
β-strand	762-765	4	9
α-helix	769-780	12

Chain B: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	16
β-strand	17-21	5	16
β-strand	29-31	3	16
β-strand	35-38	4	17
β-strand	53-54	2	17
α-helix	57-60	4
β-strand	65-68	4	17
β-strand	71	1	18
β-strand	76	1	18
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-125	13
β-strand	131-136	6	16
α-helix	137-144	8
β-strand	152-155	4	19
β-strand	160-163	4	19
β-strand	165-166	2	20
β-strand	169-170	2	20
α-helix	172-174	3
β-strand	176-178	3	19
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-243	6	21
β-strand	245-250	6	21
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	19
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	367-371	5

Chain C: 24 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-9	2	22
β-strand	17-19	3	23
β-strand	20-21	2	22
β-strand	29-31	3	23
β-strand	35-38	4	24
β-strand	53-54	2	24
α-helix	57-60	4
α-helix	62-64	3
β-strand	65-68	4	24
β-strand	71	1	25
β-strand	76	1	25
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	22
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	22
α-helix	137-145	9
β-strand	152-155	4	26
β-strand	160-163	4	26
β-strand	165-166	2	27
β-strand	169-170	2	27
α-helix	172-174	3
β-strand	176-178	3	26
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-242	5	28
β-strand	245-250	6	28
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	26
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	26
α-helix	338-347	10
α-helix	350-352	3
β-strand	357-358	2	22
α-helix	359-365	7
α-helix	367-371	5

Chain D: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	29
β-strand	17-21	5	29
β-strand	29-31	3	29
β-strand	35-38	4	30
β-strand	53-54	2	30
α-helix	56-60	5
β-strand	65-68	4	30
β-strand	71	1	31
β-strand	76	1	31
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	29
α-helix	113-125	13
β-strand	131-136	6	29
α-helix	137-144	8
β-strand	152-155	4	32
β-strand	160-163	4	32
β-strand	165-166	2	33
β-strand	169-170	2	33
α-helix	172-174	3
β-strand	176-178	3	32
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-240	3	34
β-strand	248-250	3	34
α-helix	253-256	4
α-helix	257-261	5
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	32
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	32
α-helix	338-348	11
α-helix	351-355	5
β-strand	357-358	2	29
α-helix	359-365	7
α-helix	366-371	6

Chain E: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	35
β-strand	17-21	5	35
β-strand	29-31	3	35
β-strand	35-38	4	36
β-strand	53-54	2	36
α-helix	55-61	7
β-strand	65-68	4	36
β-strand	71	1	37
β-strand	76	1	37
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	35
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	35
α-helix	137-145	9
β-strand	150-155	6	38
β-strand	160-166	7	38
β-strand	169-170	2	38
α-helix	172-174	3
β-strand	176-178	3	38
α-helix	182-193	12
α-helix	205-216	12
α-helix	223-232	10
β-strand	238-240	3	39
β-strand	248-250	3	39
α-helix	253-256	4
α-helix	257-261	5
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	38
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	38
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	35
α-helix	359-365	7
α-helix	366-371	6

Chain F: 21 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	10
β-strand	17-21	5	10
β-strand	29-31	3	10
β-strand	35-38	4	11
β-strand	53-54	2	11
α-helix	57-60	4
β-strand	65-68	4	11
β-strand	71	1	12
β-strand	76	1	12
α-helix	79-88	10
α-helix	89-93	5
β-strand	103-107	5	10
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	10
α-helix	137-144	8
β-strand	152-155	4	13
β-strand	160-163	4	13
β-strand	165-166	2	14
β-strand	169-170	2	14
α-helix	172-174	3
β-strand	176-178	3	13
α-helix	182-193	12
α-helix	203-216	14
α-helix	224-232	9
β-strand	238-242	5	15
β-strand	245-250	6	15
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	13
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	13
α-helix	338-348	11
α-helix	353-355	3
β-strand	357-358	2	10
α-helix	359-365	7
α-helix	367-371	5

Chain O: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	46-209	164

Chain P: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	46-207	162

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
beta-cardiac myosin II	A	protein	865	Homo sapiens	P12883 (AlphaFold model)
Actin, alpha cardiac muscle 1	B, C, D, E, F	protein	377	Sus scrofa	P68137 (AlphaFold model)
Tropomyosin alpha-1 chain	O, P	protein	284	Homo sapiens	P09493 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8EFH_1 beta-cardiac myosin II (chains A)
MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVT
AETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGL
FCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES
GAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDN
SSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM
LLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFG
NMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV
IYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINF
TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMF
PKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDP
LNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMT
NLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ
RYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDER
LSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLL
KSGLNDIFEAQKIEWHEDYKDDDDK

Sequence of entity 2 (B, C, D, E, F), FASTA

>8EFH_2 Actin, alpha cardiac muscle 1 (chains B, C, D, E, F)
MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
LSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIS
KQEYDEAGPSIVHRKCF

Sequence of entity 3 (O, P), FASTA

>8EFH_3 Tropomyosin alpha-1 chain (chains O, P)
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKY
SEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA
DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE
ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE
FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6
MG	Magnesium ion	Mg	6

Primary citation

Conformational changes linked to ADP release from human cardiac myosin bound to actin-tropomyosin. Doran, M.H., Rynkiewicz, M.J., Rassici, D. et al. J Gen Physiol (2023) 155. DOI 10.1085/jgp.202213267 · 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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