6X5Z: Bovine Cardiac Myosin

Bovine Cardiac Myosin in Complex with Chicken Skeletal Actin and Human Cardiac Tropomyosin in the Rigor State. Determined by electron microscopy at 4.24 Å resolution. Released 22 Jul 2020.

Method: Electron microscopy
Resolution: 4.24 Å
Organisms: Gallus gallus, Homo sapiens, Bos taurus
Chains: 8
Atoms: 28,416
Mol. weight: 485.51 kDa
Ligands: MG, ADP
Released: 22 Jul 2020

Explore 6X5Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6X5Z contains 167 α-helices and 151 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: 20 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	9-10	2	19
β-strand	16-20	5	19
β-strand	29-32	4	19
β-strand	35-38	4	20
β-strand	53-54	2	20
α-helix	55-60	6
α-helix	62-64	3
β-strand	65-68	4	20
β-strand	71-72	2	21
β-strand	75-76	2	21
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	22
α-helix	114-125	12
β-strand	131-136	6	22
α-helix	137-145	9
β-strand	150-153	4	3
β-strand	160	1	23
β-strand	162-166	5	3
β-strand	169-170	2	3
α-helix	172-174	3
β-strand	178	1	23
α-helix	182-193	12
α-helix	203-215	13
α-helix	223-232	10
β-strand	238-241	4	24
β-strand	247-250	4	24
α-helix	253-256	4
α-helix	259-262	4
α-helix	274-283	10
α-helix	290-293	4
β-strand	297-299	3	3
α-helix	309-320	12
β-strand	329-330	2	3
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	22
α-helix	359-365	7
α-helix	369-372	4

Chain B: 20 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	9-10	2	1
β-strand	16-20	5	1
β-strand	29-32	4	1
β-strand	35-38	4	2
β-strand	42	1	3
β-strand	53-54	2	2
α-helix	55-60	6
α-helix	62-64	3
β-strand	65-68	4	2
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	5
α-helix	114-125	12
β-strand	131-136	6	5
α-helix	137-145	9
β-strand	150-153	4	6
β-strand	160	1	7
β-strand	162-166	5	6
β-strand	169-170	2	6
α-helix	172-174	3
β-strand	178	1	7
α-helix	182-193	12
α-helix	203-215	13
α-helix	223-232	10
β-strand	238-241	4	8
β-strand	247-250	4	8
α-helix	253-256	4
α-helix	259-262	4
α-helix	274-283	10
α-helix	290-293	4
β-strand	297-299	3	6
α-helix	309-320	12
β-strand	329-330	2	6
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	5
α-helix	359-365	7
α-helix	369-372	4

Chain C: 20 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	9-10	2	35
β-strand	16-20	5	35
β-strand	29-32	4	35
β-strand	35-38	4	36
β-strand	53-54	2	36
α-helix	55-60	6
α-helix	62-64	3
β-strand	65-68	4	36
β-strand	71-72	2	37
β-strand	75-76	2	37
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	38
α-helix	114-125	12
β-strand	131-136	6	38
α-helix	137-144	8
β-strand	150-153	4	39
β-strand	160	1	40
β-strand	162-166	5	39
β-strand	169-170	2	39
α-helix	172-174	3
β-strand	178	1	40
α-helix	182-193	12
α-helix	203-215	13
α-helix	223-232	10
β-strand	238-241	4	41
β-strand	247-250	4	41
α-helix	253-256	4
α-helix	259-262	4
α-helix	274-283	10
α-helix	290-293	4
β-strand	297-299	3	39
α-helix	309-320	12
β-strand	329-330	2	39
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	38
α-helix	359-365	7
α-helix	369-372	4

Chains D, G and J: 35 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	37-39	3	25
β-strand	47-49	3	25
β-strand	51-55	5	26
β-strand	58-62	5	26
β-strand	68-72	5	26
β-strand	77-78	2	25
α-helix	79-81	3
β-strand	89	1	27
α-helix	98-110	13
β-strand	116-118	3	27
β-strand	121-123	3	27
α-helix	132-134	3
α-helix	136-139	4
α-helix	154-168	15
β-strand	172-176	5	28
α-helix	180-182	3
α-helix	188-197	10
α-helix	219-229	11
β-strand	232-233	2	29
β-strand	241-242	2	29
β-strand	245-252	8	28
β-strand	258-260	3	28
β-strand	263-266	4	28
α-helix	270-273	4
β-strand	283	1	29
α-helix	284-290	7
α-helix	295-301	7
α-helix	307-309	3
α-helix	311-314	4
α-helix	325-338	14
α-helix	343-358	16
α-helix	359-361	3
β-strand	363-366	4	30
α-helix	367	1
β-strand	373-376	4	30
α-helix	378-387	10
α-helix	392-400	9
α-helix	417-446	30
β-strand	455-461	7	28
α-helix	463-465	3
β-strand	471	1	31
α-helix	473-503	31
α-helix	515-525	11
α-helix	531-539	9
α-helix	545-556	12
β-strand	557	1	32
β-strand	560	1	32
β-strand	563-564	2	31
β-strand	577-579	3	31
β-strand	586-588	3	31
α-helix	593-597	5
α-helix	603-608	6
α-helix	614-621	8
α-helix	647-663	17
β-strand	667-670	4	28
α-helix	686-696	11
α-helix	698-707	10
β-strand	710	1	33
β-strand	713-714	2	34
α-helix	715-721	7
α-helix	738-740	3
α-helix	751-752	2
β-strand	762-763	2	34
β-strand	765	1	33
α-helix	772-775	4

Chains O and P: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	46-209	164

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C	protein	377	Gallus gallus	P68139 (AlphaFold model)
Tropomyosin alpha-1 chain	O, P	protein	284	Homo sapiens	P09493 (AlphaFold model)
Myosin-7	D, G, J	protein	850	Bos taurus	Q9BE39 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>6X5Z_1 Actin, alpha skeletal muscle (chains A, B, C)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (O, P), FASTA

>6X5Z_2 Tropomyosin alpha-1 chain (chains O, P)
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKY
SEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA
DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE
ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE
FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI

Sequence of entity 3 (D, G, J), FASTA

>6X5Z_3 Myosin-7 (chains D, G, J)
MVDAEMAAFGEAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKEEFVKATILSREGGKVT
AETEHGKTVTVKEDQVLQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGL
FCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES
GAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDN
SSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM
LLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFG
NMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV
VYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINF
TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMF
PKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDP
LNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSALHRENLNKLMT
NLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ
RYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDER
LSRIITRIQAQSRGVLSRMEFKKLLERRDSLLIIQWNIRAFMGVKNWPWMKLYFKIKPLL
KSAETEKEIA

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	3
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	3

Primary citation

Cryo-EM and Molecular Docking Shows Myosin Loop 4 Contacts Actin and Tropomyosin on Thin Filaments. Doran, M.H., Pavadai, E., Rynkiewicz, M.J. et al. Biophys J (2020) 119:821-830. DOI 10.1016/j.bpj.2020.07.006 · PubMed

Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7W4Z 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (AMPPNP-form)
7W50 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-Pi-form)
7W51 1.2 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-form)
9L2N 1.7 Å, Crystal structure of Cytochalasin D bound to a filamentous conformation actin
7W52 2.0 Å, Crystal structure of fragmin domain-1 (15-160) in complex with actin
1MDU 2.2 Å, Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1…
8D13 2.43 Å, Helical ADP-F-actin
8D14 2.51 Å, Helical ADP-Pi-F-actin
7R94 2.6 Å, T-Plastin-F-actin complex
8C4E 2.6 Å, F-actin decorated by SipA426-685
9JW0 2.69 Å, Structure of the N-terminal 3 domains (V1-V3) villin bound to actin
7YNE 2.7 Å, Crystal structure of fragmin domain-1 (1-160) in complex with G-form actin

Browse structure collections

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