8EFD: Beta-cardiac myosin II

Human cardiac myosin II and associated essential light chain in the rigor conformation. 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: 7,107
Mol. weight: 119.78 kDa
Released: 11 Jan 2023

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

Secondary structure: helices and β-sheets

8EFD contains 45 α-helices and 33 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: 36 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	7-12	6
α-helix	13-16	4
α-helix	22-27	6
β-strand	38	1	1
β-strand	39	1	2
β-strand	47	1	2
β-strand	49-51	3	3
β-strand	55	1	4
β-strand	58	1	4
β-strand	61-63	3	3
β-strand	77	1	1
β-strand	89	1	5
α-helix	90-92	3
α-helix	98-110	13
β-strand	115-118	4	5
β-strand	121-124	4	5
α-helix	132-134	3
α-helix	136-142	7
α-helix	151	1
α-helix	154-168	15
β-strand	172-177	6	5
α-helix	184-196	13
α-helix	217-230	14
β-strand	232-233	2	6
β-strand	241-242	2	6
β-strand	245-252	8	5
β-strand	258-266	9	5
α-helix	271-274	4
β-strand	283	1	6
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	7
α-helix	367	1
β-strand	373-374	2	7
α-helix	380-388	9
α-helix	392-400	9
β-strand	403-406	4	8
β-strand	409-412	4	8
α-helix	417-447	31
β-strand	454-461	8	5
α-helix	473-503	31
α-helix	514-525	12
α-helix	530-539	10
α-helix	545-556	12
β-strand	557	1	9
β-strand	560	1	9
β-strand	564	1	10
β-strand	577-581	5	10
β-strand	584-588	5	10
α-helix	593-597	5
α-helix	603-610	8
α-helix	616-619	4
α-helix	647-663	17
β-strand	666-671	6	5
α-helix	686-696	11
α-helix	698-706	9
β-strand	711-714	4	11
α-helix	715-722	8
α-helix	739-748	10
α-helix	753-755	3
β-strand	756-757	2	11
β-strand	762-765	4	11
α-helix	767-795	29

Chain B: 9 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	44-56	13
α-helix	66-74	9
α-helix	82-88	7
α-helix	96-99	4
α-helix	104-115	12
α-helix	123-131	9
β-strand	140-142	3	12
α-helix	143-152	10
α-helix	159-165	7
β-strand	175-177	3	12
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

>8EFD_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

>8EFD_2 Myosin light chain 1/3, skeletal muscle isoform (chains B)
MAPKKDVKKPAAAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQEDFKEAFLLFDRTG
ECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMMQAISNNKDQ
GGYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQEDSNGCINYEA
FVKHIMSV

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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