5TBY: Myosin-7

Human beta cardiac heavy meromyosin interacting-heads motif obtained by homology modeling (using swiss-model) of human sequence from aphonopelma homology model (PDB-3JBH), rigidly fitted to human beta-cardiac negatively stained thick filament 3D-reconstruction (emd-2240). Determined by electron microscopy at 20.0 Å resolution. Released 7 Jun 2017.

Method: Electron microscopy
Resolution: 20.0 Å
Organism: Homo sapiens
Chains: 6
Atoms: 20,357
Mol. weight: 528.44 kDa
Released: 7 Jun 2017

Explore 5TBY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5TBY contains 119 α-helices and 71 β-strands across 6 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, 24 β-strands

Element	Residues	Length	Sheet
α-helix	13-15	3
α-helix	26-28	3
β-strand	36-41	6	1
β-strand	45-51	7	1
β-strand	55	1	1
β-strand	58-63	6	1
β-strand	68-72	5	1
β-strand	77-78	2	1
α-helix	79-81	3
β-strand	89	1	2
α-helix	90-92	3
α-helix	98-110	13
β-strand	116-118	3	2
β-strand	121-125	5	2
α-helix	136-142	7
α-helix	147-149	3
α-helix	154-168	15
β-strand	172-177	6	2
α-helix	185-198	14
α-helix	215-229	15
β-strand	246-252	7	2
β-strand	258-264	7	2
α-helix	284-291	8
α-helix	295-300	6
α-helix	328-339	12
α-helix	343-358	16
α-helix	382-388	7
α-helix	396-399	4
β-strand	403-406	4	3
β-strand	409-412	4	3
α-helix	417-423	7
α-helix	427-447	21
β-strand	456-457	2	2
β-strand	459-461	3	2
β-strand	471	1	4
α-helix	476-490	15
α-helix	491-496	6
α-helix	497-504	8
α-helix	530-537	8
α-helix	545-554	10
β-strand	563-564	2	4
β-strand	576-580	5	4
β-strand	585-589	5	4
α-helix	593-596	4
α-helix	607-610	4
α-helix	615-620	6
α-helix	647-663	17
β-strand	666-673	8	2
α-helix	686-695	10
α-helix	698-707	10
β-strand	711-713	3	5
α-helix	717-721	5
α-helix	727-729	3
α-helix	738-748	11
β-strand	756-758	3	5
β-strand	763-765	3	5
α-helix	770-782	13
α-helix	786-800	15
α-helix	802-823	22
α-helix	837-839	3
α-helix	846-877	32
α-helix	879-958	80

Chain B: 42 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	26-31	6
β-strand	36-40	5	6
β-strand	46-50	5	6
β-strand	51-55	5	7
β-strand	58-61	4	7
β-strand	69-72	4	7
α-helix	73-75	3
β-strand	77-78	2	6
α-helix	79	1
α-helix	82-84	3
α-helix	98-110	13
β-strand	115-116	2	8
β-strand	122-125	4	8
α-helix	138-141	4
α-helix	155-168	14
β-strand	172-177	6	8
α-helix	184-198	15
α-helix	215-231	17
β-strand	232-233	2	9
β-strand	234	1	10
β-strand	241-242	2	9
β-strand	244-252	9	8
β-strand	258-268	11	8
α-helix	271-273	3
β-strand	281	1	10
α-helix	285-292	8
α-helix	295-300	6
α-helix	327-339	13
α-helix	343-358	16
α-helix	359-361	3
β-strand	364	1	11
β-strand	375	1	11
α-helix	379-388	10
α-helix	392-398	7
β-strand	403-406	4	12
β-strand	409-412	4	12
α-helix	414-416	3
α-helix	417-446	30
β-strand	455-462	8	8
α-helix	473-490	18
α-helix	491-496	6
α-helix	497-504	8
α-helix	525-528	4
α-helix	533-536	4
α-helix	545-555	11
β-strand	563-564	2	13
β-strand	576-577	2	14
β-strand	578-579	2	13
β-strand	588-589	2	14
α-helix	593-596	4
α-helix	603-610	8
α-helix	616-619	4
α-helix	647-663	17
β-strand	666	1	8
α-helix	667	1
β-strand	669-673	5	8
α-helix	686-695	10
α-helix	698-704	7
β-strand	711-714	4	15
α-helix	715-722	8
α-helix	723-725	3
α-helix	742-747	6
α-helix	753-755	3
β-strand	756-757	2	15
β-strand	762-765	4	15
α-helix	769-780	12
α-helix	783-800	18
α-helix	807-818	12
α-helix	821-824	4
α-helix	846-865	20
α-helix	869-958	90

Chain C: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	48-61	14
β-strand	70-72	3	16
α-helix	75-82	8
α-helix	89-95	7
β-strand	108-110	3	16
α-helix	111-123	13
α-helix	130-137	8
β-strand	147-149	3	17
α-helix	150-159	10
α-helix	166-172	7
β-strand	182-184	3	17
α-helix	185-194	10

Chain D: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	48-61	14
β-strand	71-72	2	18
α-helix	76-83	8
α-helix	89-94	6
β-strand	108-109	2	18
α-helix	111-121	11
α-helix	131-138	8
β-strand	147-149	3	19
α-helix	150-159	10
α-helix	166-172	7
β-strand	182-184	3	19
α-helix	185-194	10

Chain E: 11 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	27-30	4
α-helix	33-36	4
β-strand	43	1	20
α-helix	46-56	11
α-helix	63-72	10
β-strand	78	1	20
α-helix	79-87	9
α-helix	94-95	2
α-helix	96-100	5
α-helix	104-106	3
β-strand	114-115	2	21
α-helix	116-123	8
α-helix	132-140	9
β-strand	144-145	2	21
β-strand	148-149	2	21
α-helix	151-158	8

Chain F: 12 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	28-32	5
α-helix	33-35	3
β-strand	39	1	22
β-strand	43	1	22
α-helix	49-52	4
α-helix	53-55	3
α-helix	63-65	3
α-helix	66-69	4
α-helix	79-91	13
α-helix	96-99	4
α-helix	101-104	4
β-strand	114	1	23
α-helix	116-125	10
α-helix	132-141	10
β-strand	144	1	23
β-strand	149	1	23
α-helix	151-156	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin-7	A, B	protein	1935	Homo sapiens	P12883 (AlphaFold model)
Myosin light chain 3	C, D	protein	195	Homo sapiens	P08590 (AlphaFold model)
Myosin regulatory light chain 2, ventricular/cardiac muscle isoform	E, F	protein	166	Homo sapiens	P10916 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5TBY_1 Myosin-7 (chains A, B)
MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVT
AETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGL
FCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES
GAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDN
SSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM
LLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFG
NMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV
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 (C, D), FASTA

>5TBY_2 Myosin light chain 3 (chains C, D)
MAPKKPEPKKDDAKAAPKAAPAPAPPPEPERPKEVEFDASKIKIEFTPEQIEEFKEAFML
FDRTPKCEMKITYGQCGDVLRALGQNPTQAEVLRVLGKPRQEELNTKMMDFETFLPMLQH
ISKNKDTGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGERLTEDEVEKLMAGQEDSN
GCINYEAFVKHIMSS

Sequence of entity 3 (E, F), FASTA

>5TBY_3 Myosin regulatory light chain 2, ventricular/cardiac muscle isoform (chains E, F)
MAPKKAKKRAGGANSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVN
VKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGVLKADYVR
EMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD

Primary citation

Effects of myosin variants on interacting-heads motif explain distinct hypertrophic and dilated cardiomyopathy phenotypes. Alamo, L., Ware, J.S., Pinto, A. et al. Elife (2017) 6. DOI 10.7554/eLife.24634 · 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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