7JH7: Cardiac actomyosin complex

cardiac actomyosin complex. Determined by electron microscopy at 3.8 Å resolution. Released 28 Oct 2020.

Method: Electron microscopy
Resolution: 3.8 Å
Organism: Sus scrofa
Chains: 10
Atoms: 33,924
Mol. weight: 906.54 kDa
Ligands: MG, ADP
Released: 28 Oct 2020

Explore 7JH7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7JH7 contains 214 α-helices and 207 β-strands across 10 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.

Chains A and B: 22 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-9	2	1
β-strand	17-19	3	2
β-strand	20-21	2	1
β-strand	29-31	3	2
β-strand	35-38	4	3
β-strand	53-54	2	3
α-helix	55-59	5
α-helix	62-64	3
β-strand	65-68	4	3
β-strand	71	1	4
β-strand	76	1	4
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-121	9
α-helix	122-127	6
β-strand	131-136	6	1
α-helix	137-143	7
β-strand	152-155	4	5
β-strand	160-163	4	5
β-strand	165-166	2	6
β-strand	169-170	2	6
β-strand	177-178	2	5
α-helix	182-193	12
α-helix	203-205	3
α-helix	206-215	10
α-helix	224-230	7
β-strand	238-240	3	7
β-strand	248-250	3	7
α-helix	258-261	4
α-helix	264-266	3
α-helix	277-283	7
α-helix	290-295	6
β-strand	297-300	4	5
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	5
α-helix	338-346	9
α-helix	351-355	5
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	366-369	4

Chain C: 22 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-9	2	39
β-strand	18-19	2	40
β-strand	21	1	39
β-strand	29-30	2	40
β-strand	35-38	4	41
β-strand	53-54	2	41
α-helix	55-59	5
α-helix	62-64	3
β-strand	65-68	4	41
β-strand	71	1	42
β-strand	76	1	42
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	39
α-helix	113-121	9
α-helix	122-127	6
β-strand	131-136	6	39
α-helix	137-143	7
β-strand	152-155	4	43
β-strand	160-163	4	43
β-strand	165-166	2	44
β-strand	169-170	2	44
β-strand	177-178	2	43
α-helix	182-193	12
α-helix	203-205	3
α-helix	206-215	10
α-helix	224-230	7
β-strand	238-240	3	45
β-strand	248-250	3	45
α-helix	258-261	4
α-helix	264-266	3
α-helix	277-283	7
α-helix	290-295	6
β-strand	297-300	4	43
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	43
α-helix	338-346	9
α-helix	351-355	5
β-strand	357-358	2	39
α-helix	359-365	7
α-helix	366-369	4

Chain D: 22 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-9	2	65
β-strand	17-18	2	66
β-strand	20-21	2	65
β-strand	30-31	2	66
β-strand	35-38	4	67
β-strand	53-54	2	67
α-helix	55-59	5
α-helix	62-64	3
β-strand	65-68	4	67
β-strand	71	1	68
β-strand	76	1	68
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	65
α-helix	113-121	9
α-helix	122-127	6
β-strand	131-136	6	65
α-helix	137-143	7
β-strand	152-155	4	69
β-strand	160-163	4	69
β-strand	165-166	2	70
β-strand	169-170	2	70
β-strand	177-178	2	69
α-helix	182-193	12
α-helix	203-205	3
α-helix	206-215	10
α-helix	224-230	7
β-strand	238-240	3	71
β-strand	248-250	3	71
α-helix	258-261	4
α-helix	264-266	3
α-helix	277-283	7
α-helix	290-295	6
β-strand	297-300	4	69
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	69
α-helix	338-346	9
α-helix	351-355	5
β-strand	357-358	2	65
α-helix	359-365	7
α-helix	366-369	4

Chain E: 22 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-9	2	58
β-strand	17-18	2	59
β-strand	21	1	58
β-strand	30-31	2	59
β-strand	35-38	4	60
β-strand	53-54	2	60
α-helix	55-59	5
α-helix	62-64	3
β-strand	65-68	4	60
β-strand	71	1	61
β-strand	76	1	61
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	58
α-helix	113-121	9
α-helix	122-127	6
β-strand	131-136	6	58
α-helix	137-143	7
β-strand	152-155	4	62
β-strand	160-163	4	62
β-strand	165-166	2	63
β-strand	169-170	2	63
β-strand	177-178	2	62
α-helix	182-193	12
α-helix	203-205	3
α-helix	206-215	10
α-helix	224-230	7
β-strand	238-240	3	64
β-strand	248-250	3	64
α-helix	258-261	4
α-helix	264-266	3
α-helix	277-283	7
α-helix	290-295	6
β-strand	297-300	4	62
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	62
α-helix	338-346	9
α-helix	351-355	5
β-strand	357-358	2	58
α-helix	359-365	7
α-helix	366-369	4

Chains F and H: 34 helices, 34 β-strands

Element	Residues	Length	Sheet
α-helix	14-17	4
α-helix	23-26	4
β-strand	36-39	4	8
α-helix	40	1
β-strand	47-51	5	8
β-strand	58-60	3	9
β-strand	61-63	3	8
β-strand	70-72	3	9
β-strand	77-78	2	8
β-strand	89	1	10
α-helix	99-110	12
β-strand	115-118	4	10
β-strand	121-124	4	10
α-helix	136-139	4
α-helix	151	1
α-helix	154-167	14
β-strand	172-177	6	11
α-helix	184-197	14
α-helix	217-231	15
β-strand	232-233	2	12
β-strand	241-242	2	12
β-strand	245	1	13
β-strand	246-252	7	11
β-strand	258-263	6	11
β-strand	266	1	13
α-helix	270-274	5
α-helix	284-290	7
α-helix	295-300	6
α-helix	325-337	13
α-helix	344-357	14
β-strand	365-366	2	14
α-helix	367	1
β-strand	373-374	2	14
α-helix	380-388	9
α-helix	392-400	9
β-strand	403-406	4	15
β-strand	409-412	4	15
α-helix	417-447	31
β-strand	454	1	11
β-strand	457-462	6	11
α-helix	473-504	32
α-helix	515-524	10
α-helix	530-537	8
α-helix	545-556	12
β-strand	557	1	16
β-strand	560	1	16
β-strand	563-564	2	17
α-helix	565-567	3
β-strand	577-581	5	17
β-strand	584-588	5	17
α-helix	593-597	5
β-strand	598-599	2	18
α-helix	603-611	9
α-helix	616-619	4
β-strand	645-646	2	18
α-helix	647-662	16
β-strand	666	1	11
β-strand	670-671	2	11
α-helix	686-695	10
α-helix	698-706	9
β-strand	711-714	4	19
α-helix	715-721	7
α-helix	738-746	9
α-helix	753-755	3
β-strand	756-758	3	19
β-strand	762-765	4	19
α-helix	772-775	4
α-helix	777-780	4

Chain G: 34 helices, 34 β-strands

Element	Residues	Length	Sheet
α-helix	14-17	4
α-helix	23-26	4
β-strand	36-39	4	27
α-helix	40	1
β-strand	47-51	5	27
β-strand	58-60	3	28
β-strand	61-63	3	27
β-strand	70-72	3	28
β-strand	77-78	2	27
β-strand	89	1	29
α-helix	99-110	12
β-strand	115-118	4	29
β-strand	121-124	4	29
α-helix	136-139	4
α-helix	151	1
α-helix	154-167	14
β-strand	172-177	6	30
α-helix	184-197	14
α-helix	217-231	15
β-strand	232-233	2	31
β-strand	241-242	2	31
β-strand	245	1	32
β-strand	246-252	7	30
β-strand	258-263	6	30
β-strand	266	1	32
α-helix	270-274	5
α-helix	284-290	7
α-helix	295-300	6
α-helix	325-337	13
α-helix	344-357	14
β-strand	365-366	2	33
α-helix	367	1
β-strand	373-374	2	33
α-helix	380-388	9
α-helix	392-400	9
β-strand	403-406	4	34
β-strand	409-412	4	34
α-helix	417-447	31
β-strand	454	1	30
β-strand	457-462	6	30
α-helix	473-504	32
α-helix	515-524	10
α-helix	530-537	8
α-helix	545-556	12
β-strand	557	1	35
β-strand	560	1	35
β-strand	563-564	2	36
α-helix	565-567	3
β-strand	577-581	5	36
β-strand	584-588	5	36
α-helix	593-597	5
β-strand	598	1	37
α-helix	603-611	9
α-helix	616-619	4
β-strand	646	1	37
α-helix	647-662	16
β-strand	666	1	30
β-strand	670-671	2	30
α-helix	686-695	10
α-helix	698-706	9
β-strand	711-714	4	38
α-helix	715-721	7
α-helix	738-746	9
α-helix	753-755	3
β-strand	756-758	3	38
β-strand	762-765	4	38
α-helix	772-775	4
α-helix	777-780	4

Chains I and J: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	63-195	133

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha cardiac muscle 1	A, B, C, D, E	protein	377	Sus scrofa	B6VNT8 (AlphaFold model)
Myosin-7	F, G, H	protein	1935	Sus scrofa	P79293 (AlphaFold model)
tropomyosin	I, J	protein	135	Sus scrofa

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

>7JH7_1 Actin, alpha cardiac muscle 1 (chains A, B, C, D, E)
MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
LSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIS
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (F, G, H), FASTA

>7JH7_2 Myosin-7 (chains F, G, H)
MVDAEMAAFGEAAPYLRKSEKERLEAQTRPFDLKKDVYVPDDKEEFVKAKILSREGGKVT
AETEHGKTVTVKEDQVLQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGL
FCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES
GAGKTVNTKRVIQYFAVIAAIGDRSKKEQTPGKGTLEDQIIQANPALEAFGNAKTVRNDN
SSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM
LLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFG
NMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV
MYATGALAKAVYEKMFNWMVTRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINF
TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMF
PKATDMTFKAKLYDNHLGKSNNFQKPRNIKGRPEAHFALIHYAGTVDYNIIGWLQKNKDP
LNETVVDLYKKSSLKLLSNLFANYAGADTPVEKGKGKAKKGSSFQTVSALHRENLNKLMT
NLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ
RYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDER
LSRIITRIQAQSRGVLSRMEFKKLLERRDSLLIIQWNIRAFMSVKNWPWMKLYFKIKPLL
KSAETEKEMATMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLAD
AEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELT
LAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTL
TKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERL
KKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLS
RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSV
AELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHR
SKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE
EEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAI
QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAA
ALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKR
ENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILR
AQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG
DLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNL
LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTE
VEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEA
EQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKN
LLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL
RAKSRDIGTKGLNEE

Sequence of entity 3 (I, J), FASTA

>7JH7_3 tropomyosin (chains I, J)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXX

Ligands and cofactors

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

Primary citation

High-Resolution Cryo-EM Structure of the Cardiac Actomyosin Complex. Risi, C., Schafer, L.U., Belknap, B. et al. Structure (2021) 29:50. DOI 10.1016/j.str.2020.09.013 · PubMed

Other PDB entries of the same protein (UniProt B6VNT8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8EFI 3.4 Å, Helical reconstruction of the human cardiac actin-tropomyosin-myosin complex in the…
8ENC 3.6 Å, Helical reconstruction of the human cardiac actin-tropomyosin-myosin loop 4 7G mutant…
9YA8 4.32 Å, The structure of the cardiac native crossbridge in the rigor state, myosin heads bound…
9YK9 4.5 Å, The structure of the cardiac native crossbridge in the rigor state, myosin heads bound…
9YAQ 4.63 Å, The structure of the cardiac native cross bridge in the rigor state, myosin heads bound…
9YJP 4.8 Å, The structure of the cardiac native crossbridge in the rigor state, myosin heads bound…
9YKN 5.3 Å, The structure of the cardiac native crossbridge in the rigor state, myosin heads with…
7LRG 6.1 Å, Filamentous actin decorated with human cardiac myosin binding protein C C2 domain

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