9MOC: Actin, alpha cardiac muscle 1

Structure of native murine cardiac thin filament variant I79N in troponin T at pCa=5.8 in Ca2+-free rotated state (upper strand). Determined by electron microscopy at 5.6 Å resolution. Released 28 May 2025.

Method: Electron microscopy
Resolution: 5.6 Å
Organism: Mus musculus
Chains: 15
Atoms: 28,811
Mol. weight: 540.62 kDa
Ligands: ADP, MG
Released: 28 May 2025

Explore 9MOC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9MOC contains 176 α-helices and 153 β-strands across 15 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, B, C, D, E and G: 22 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8	1	1
β-strand	11	1	2
β-strand	17-19	3	2
β-strand	21	1	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	113-125	13
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	5
β-strand	160-166	7	5
β-strand	169-170	2	5
α-helix	172-174	3
β-strand	176-178	3	5
α-helix	182-192	11
α-helix	193-195	3
α-helix	205-216	12
α-helix	223-230	8
β-strand	238-242	5	6
β-strand	245-250	6	6
α-helix	258-261	4
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	5
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	5
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3

Chain F: 22 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8	1	31
β-strand	11	1	32
β-strand	17-19	3	32
β-strand	21	1	31
β-strand	24	1	33
β-strand	29-31	3	32
β-strand	35-38	4	34
β-strand	53-54	2	34
α-helix	55-59	5
α-helix	62-64	3
β-strand	65-68	4	34
β-strand	71	1	35
β-strand	76	1	35
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	31
α-helix	113-125	13
β-strand	131-136	6	31
α-helix	137-144	8
β-strand	150-155	6	36
β-strand	160-166	7	36
β-strand	169-170	2	36
α-helix	172-174	3
β-strand	176-178	3	36
α-helix	182-192	11
α-helix	193-195	3
α-helix	205-216	12
α-helix	223-230	8
β-strand	238-242	5	37
β-strand	245-250	6	37
α-helix	258-261	4
α-helix	274-283	10
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	338-347	10
α-helix	351-354	4
β-strand	357-358	2	31
α-helix	359-365	7
α-helix	367-369	3

Chain H: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	3-10	8
α-helix	14-27	14
α-helix	38-47	10
α-helix	54-62	9
α-helix	74-84	11
β-strand	91	1	44
α-helix	94-104	11
β-strand	112	1	45
α-helix	114-123	10
α-helix	134-140	7
β-strand	148	1	45
α-helix	150-156	7
β-strand	159	1	44

Chain I: 6 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	44-80	37
α-helix	82-84	3
α-helix	91-137	47
α-helix	142-144	3
α-helix	152-154	3
α-helix	157-184	28
β-strand	185	1	33

Chain J: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	201-213	13
α-helix	226-270	45

Chain K: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	89-149	61

Chain L: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	65-283	219

Chain M: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	65-281	217

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha cardiac muscle 1	A, B, C, D, E, F, G	protein	377	Mus musculus	P68033 (AlphaFold model)
Troponin C, slow skeletal and cardiac muscles	H	protein	161	Mus musculus	P19123 (AlphaFold model)
Troponin I, cardiac muscle	I	protein	211	Mus musculus	P48787 (AlphaFold model)
Isoform 6 of Troponin T, cardiac muscle	J, K	protein	288	Mus musculus	P45379 (AlphaFold model)
Tropomyosin alpha-1 chain	L, M, N, O	protein	284	Mus musculus	P58771

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

>9MOC_1 Actin, alpha cardiac muscle 1 (chains A, B, C, D, E, F, G)
MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
LSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIS
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (H), FASTA

>9MOC_2 Troponin C, slow skeletal and cardiac muscles (chains H)
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEM
IDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKMM
LQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE

Sequence of entity 3 (I), FASTA

>9MOC_3 Troponin I, cardiac muscle (chains I)
MADESSDAAGEPQPAPAPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQ
EMEREAEERRGEKGRVLRTRCQPLELDGLGFEELQDLCRQLHARVDKVDEERYDVEAKVT
KNITEIADLTQKIYDLRGKFKRPTLRRVRISADAMMQALLGTRAKESLDLRAHLKQVKKE
DIEKENREVGDWRKNIDALSGMEGRKKKFEG

Sequence of entity 4 (J, K), FASTA

>9MOC_4 Isoform 6 of Troponin T, cardiac muscle (chains J, K)
MSDIEEVVEEYEEEEQEEAAVEEQEEAAEEDAEAEAETEETRAEEDEEEEEAKEAEDGPM
EESKPKPRSFMPNLVPPKNPDGERVDFDDIHRKRMEKDLNELQALIEAHFENRKKEEEEL
VSLKDRIERRRAERAEQQRIRNEREKERQNRLAEERARREEEENRRKAEDEARKKKALSN
MMHFGGYIQKQAQTERKSGKRQTEREKKKKILAERRKVLAIDHLNEDQLREKAKELWQSI
YNLEAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK

Sequence of entity 5 (L, M, N, O), FASTA

>9MOC_5 Tropomyosin alpha-1 chain (chains L, M, N, O)
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKY
SEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA
DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE
ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE
FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	7
MG	Magnesium ion	Mg	7

Primary citation

The role of the troponin T interactions with actin in regulation of cardiac thin filament revealed by the troponin T pathogenic variant Ile79Asn. Risi, C.M., Landim-Vieira, M., Belknap, B. et al. J Mol Cell Cardiol (2025) 204:55-67. DOI 10.1016/j.yjmcc.2025.05.005 · PubMed

Other PDB entries of the same protein (UniProt P68033 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8ZBN 3.02 Å, Mouse MYH6 R404Q left ventricle ATM complex
8ZIU 3.54 Å, Mouse MYH6 R404Q left ventricle actin and myosin complex
9E2E 4.0 Å, The structure of the junction region of the wild-type murine native cardiac thin…
8ZBK 4.28 Å, Mouse left ventricle ATM complex
8ZIP 4.9 Å, Mouse left ventricle actin and myosin complex
9MOW 4.9 Å, Structure of native murine cardiac thin filament variant I79N in troponin T at pCa=5.8…
9MOP 5.0 Å, Structure of native murine cardiac thin filament variant I79N in troponin T at pCa=5.8…
9MOM 5.1 Å, Structure of native murine cardiac thin filament at pCa=5.8 in Ca2+-bound partially…
9MO7 5.2 Å, Structure of native murine cardiac thin filament at pCa=5.8 in Ca2+-bound fully…
9MO8 5.2 Å, Structure of native murine cardiac thin filament at pCa=5.8 in Ca2+-free state (upper…
9MOL 5.2 Å, Structure of native murine cardiac thin filament at pCa=5.8 in Ca2+-free tilted state…
9MON 5.2 Å, Structure of native murine cardiac thin filament at pCa=5.8 in Ca2+-bound fully…

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