8EFE: Human beta-cardiac myosin II

Human beta-cardiac myosin II bound to ADP-MG2+ and the associated essential light chain. Determined by electron microscopy at 3.8 Å resolution. Released 11 Jan 2023.

Method: Electron microscopy
Resolution: 3.8 Å
Organisms: Homo sapiens, Mus musculus
Chains: 2
Atoms: 7,135
Mol. weight: 120.23 kDa
Ligands: ADP, MG
Released: 11 Jan 2023

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

Secondary structure: helices and β-sheets

8EFE contains 47 α-helices and 32 β-strands across 2 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: 38 helices, 27 β-strands

Element	Residues	Length	Sheet
α-helix	10-12	3
α-helix	13-16	4
α-helix	20-27	8
β-strand	36-39	4	1
β-strand	47-55	9	1
β-strand	58-63	6	1
β-strand	70-72	3	1
α-helix	73-75	3
β-strand	77	1	1
α-helix	82-84	3
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	154-168	15
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	284-290	7
α-helix	295-300	6
α-helix	307-309	3
α-helix	311-314	4
α-helix	326-337	12
α-helix	343-358	16
α-helix	359-361	3
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
α-helix	473-504	32
α-helix	518-525	8
α-helix	530-539	10
α-helix	545-556	12
β-strand	564	1	6
β-strand	577-580	4	6
β-strand	585-588	4	6
α-helix	593-597	5
α-helix	604-610	7
α-helix	616-619	4
α-helix	647-663	17
β-strand	666	1	2
β-strand	669-673	5	2
α-helix	686-696	11
α-helix	698-707	10
β-strand	711-714	4	7
α-helix	715-721	7
α-helix	722-724	3
α-helix	740-748	9
β-strand	756-757	2	7
β-strand	762-765	4	7
α-helix	767-795	29

Chain B: 9 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	44-56	13
β-strand	63-65	3	8
α-helix	69-75	7
α-helix	82-88	7
α-helix	94-97	4
β-strand	101-103	3	8
α-helix	104-114	11
α-helix	123-131	9
β-strand	140-142	3	9
α-helix	143-152	10
α-helix	159-166	8
β-strand	170	1	9
β-strand	175-177	3	9
α-helix	178-187	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-cardiac myosin II	A	protein	865	Homo sapiens	P12883 (AlphaFold model)
Myosin light chain 1/3, skeletal muscle isoform	B	protein	188	Mus musculus	P05977 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8EFE_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), FASTA

>8EFE_2 Myosin light chain 1/3, skeletal muscle isoform (chains B)
MAPKKDVKKPAAAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQEDFKEAFLLFDRTG
ECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMMQAISNNKDQ
GGYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQEDSNGCINYEA
FVKHIMSV

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
MG	Magnesium ion	Mg	1

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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