8ENC: Myosin-7

Helical reconstruction of the human cardiac actin-tropomyosin-myosin loop 4 7G mutant complex. Determined by electron microscopy at 3.6 Å resolution. Released 23 Nov 2022.

Method: Electron microscopy
Resolution: 3.6 Å
Organisms: Homo sapiens, Sus scrofa
Chains: 8
Atoms: 23,220
Mol. weight: 501.04 kDa
Ligands: ADP, MG
Released: 23 Nov 2022

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

Secondary structure: helices and β-sheets

8ENC contains 155 α-helices and 127 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 B: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	11
β-strand	17-21	5	11
β-strand	29-31	3	11
β-strand	35-38	4	12
β-strand	53-54	2	12
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	12
β-strand	71	1	13
β-strand	76	1	13
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	11
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	11
α-helix	137-144	8
β-strand	151-155	5	14
β-strand	160-164	5	14
β-strand	165-166	2	15
β-strand	169-170	2	15
α-helix	172-174	3
β-strand	176-178	3	14
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-242	5	16
β-strand	245-250	6	16
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	14
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	14
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	367-369	3

Chain C: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	17
β-strand	17-21	5	17
β-strand	29-31	3	17
β-strand	35-38	4	18
β-strand	53-54	2	18
α-helix	56-60	5
β-strand	65-68	4	18
β-strand	71	1	19
β-strand	76	1	19
α-helix	80-88	9
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	17
α-helix	113-125	13
β-strand	131-136	6	17
α-helix	137-145	9
β-strand	150-155	6	20
β-strand	160-166	7	20
β-strand	169-170	2	20
α-helix	172-174	3
β-strand	176-178	3	20
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-242	5	21
β-strand	245-250	6	21
α-helix	253-256	4
α-helix	259-262	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	20
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	20
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	17
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	22
β-strand	17-21	5	22
β-strand	29-31	3	22
β-strand	35-38	4	23
β-strand	53-54	2	23
α-helix	56-59	4
β-strand	65-68	4	23
β-strand	71	1	24
β-strand	76	1	24
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	22
α-helix	113-125	13
β-strand	131-136	6	22
α-helix	137-145	9
β-strand	152-155	4	25
β-strand	160-163	4	25
β-strand	165-166	2	26
β-strand	169-170	2	26
α-helix	172-174	3
β-strand	176-178	3	25
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-240	3	27
β-strand	248-250	3	27
α-helix	253-256	4
α-helix	259-262	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	25
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	25
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	22
α-helix	359-365	7
α-helix	367-371	5

Chain E: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	28
β-strand	17-21	5	28
β-strand	29-31	3	28
β-strand	35-38	4	29
β-strand	53-54	2	29
α-helix	55-61	7
β-strand	65-68	4	29
β-strand	71	1	30
β-strand	76	1	30
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	28
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	28
α-helix	137-145	9
β-strand	150-155	6	31
β-strand	160-166	7	31
β-strand	169-170	2	31
α-helix	172-174	3
β-strand	176-178	3	31
α-helix	182-193	12
α-helix	194-196	3
α-helix	205-216	12
α-helix	224-232	9
β-strand	238-240	3	32
β-strand	248-250	3	32
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	31
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	31
α-helix	338-347	10
α-helix	351-355	5
β-strand	357-358	2	28
α-helix	359-365	7
α-helix	367-371	5

Chain F: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	33
β-strand	17-21	5	33
β-strand	29-31	3	33
β-strand	35-38	4	34
β-strand	53-54	2	34
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	34
β-strand	71	1	35
β-strand	76	1	35
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	33
α-helix	113-125	13
β-strand	131-136	6	33
α-helix	137-144	8
β-strand	151-155	5	36
β-strand	160-164	5	36
β-strand	165-166	2	37
β-strand	169-170	2	37
α-helix	172-174	3
β-strand	176-178	3	36
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-242	5	38
β-strand	245-250	6	38
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	287-289	3
α-helix	290-295	6
β-strand	297-300	4	36
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	36
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	33
α-helix	359-365	7
α-helix	367-371	5

Chain M: 39 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	7-12	6
α-helix	13-16	4
α-helix	20-27	8
β-strand	38	1	1
β-strand	39-40	2	2
β-strand	46-47	2	2
β-strand	49-55	7	3
β-strand	58-63	6	3
α-helix	73-75	3
β-strand	77	1	1
α-helix	82-84	3
β-strand	89	1	4
α-helix	90-92	3
α-helix	98-110	13
β-strand	115-118	4	4
β-strand	121-125	5	4
α-helix	126-127	2
α-helix	132-134	3
α-helix	136-142	7
α-helix	151	1
α-helix	154-167	14
β-strand	172-177	6	4
α-helix	184-198	15
α-helix	217-231	15
β-strand	232-233	2	5
β-strand	241-242	2	5
β-strand	247-252	6	4
β-strand	258-264	7	4
α-helix	271-274	4
β-strand	283	1	5
α-helix	284-289	6
α-helix	295-301	7
α-helix	311-314	4
α-helix	325-337	13
α-helix	343-358	16
α-helix	359-361	3
β-strand	364-366	3	6
β-strand	373-375	3	6
α-helix	379-388	10
α-helix	392-400	9
β-strand	403-406	4	7
β-strand	409-412	4	7
α-helix	417-447	31
β-strand	456-462	7	4
α-helix	473-504	32
α-helix	515-521	7
α-helix	530-539	10
α-helix	545-556	12
β-strand	563-564	2	8
β-strand	577-581	5	8
β-strand	584-588	5	8
α-helix	593-597	5
β-strand	598	1	9
α-helix	603-611	9
α-helix	616-619	4
β-strand	646	1	9
α-helix	647-662	16
β-strand	666-673	8	4
α-helix	686-696	11
α-helix	698-706	9
β-strand	711-714	4	10
α-helix	715-722	8
α-helix	723-725	3
α-helix	739-747	9
α-helix	753-755	3
β-strand	756-757	2	10
β-strand	762-765	4	10
α-helix	767-780	14

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
Myosin-7	M	protein	1935	Homo sapiens	P12883 (AlphaFold model)
Actin, alpha cardiac muscle 1	B, C, D, E, F	protein	377	Sus scrofa	B6VNT8 (AlphaFold model)
Tropomyosin alpha-1 chain	O, P	protein	284	Homo sapiens	P09493 (AlphaFold model)

Sequence of entity 1 (M), FASTA

>8ENC_1 Myosin-7 (chains M)
MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVT
AETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGL
FCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES
GAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDN
SSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM
LLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFG
NMKFKGGGGGGGAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV
IYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINF
TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMF
PKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDP
LNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMT
NLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ
RYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDER
LSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLL
KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLAD
AEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELT
LAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTL
TKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERL
KKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLS
RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSV
AELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHR
SKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE
EEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAI
QRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAA
ALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKR
ENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILR
AQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG
DLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNL
LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTE
VEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEA
EQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKN
LLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL
RAKSRDIGTKGLNEE

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

>8ENC_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

>8ENC_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	5
MG	Magnesium ion	Mg	5

Primary citation

Myosin loop-4 is critical for optimal tropomyosin repositioning on actin during muscle activation and relaxation. Doran, M.H., Rynkiewicz, M.J., Pavadai, E. et al. J Gen Physiol (2023) 155. DOI 10.1085/jgp.202213274 · 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

About this viewer

MolViewer shows 8ENC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.