9MO9: 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 (lower 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
- 14
- Atoms
- 25,887
- Mol. weight
- 498.11 kDa
- Ligands
- MG, ADP
- Released
- 28 May 2025
Explore 9MO9 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9MO9 contains 155 α-helices and 128 β-strands across 14 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 and F: 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 E: 22 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8 | 1 | 25 |
| β-strand | 11 | 1 | 26 |
| β-strand | 17-19 | 3 | 26 |
| β-strand | 21 | 1 | 25 |
| β-strand | 24 | 1 | 27 |
| β-strand | 29-31 | 3 | 26 |
| β-strand | 35-38 | 4 | 28 |
| β-strand | 53-54 | 2 | 28 |
| α-helix | 55-59 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 28 |
| β-strand | 71 | 1 | 29 |
| β-strand | 76 | 1 | 29 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-94 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 25 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 25 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 30 |
| β-strand | 160-166 | 7 | 30 |
| β-strand | 169-170 | 2 | 30 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 30 |
| 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 | 31 |
| β-strand | 245-250 | 6 | 31 |
| α-helix | 258-261 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 30 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 30 |
| α-helix | 338-347 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 25 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-369 | 3 | |
Chain G: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-10 | 7 | |
| α-helix | 14-27 | 14 | |
| α-helix | 38-47 | 10 | |
| α-helix | 54-63 | 10 | |
| α-helix | 74-84 | 11 | |
| α-helix | 94-104 | 11 | |
| α-helix | 114-124 | 11 | |
| α-helix | 135-140 | 6 | |
| α-helix | 150-157 | 8 | |
Chain H: 6 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 47-80 | 34 | |
| α-helix | 82-85 | 4 | |
| α-helix | 91-137 | 47 | |
| α-helix | 138-140 | 3 | |
| α-helix | 152-154 | 3 | |
| α-helix | 158-184 | 27 | |
| β-strand | 185 | 1 | 27 |
Chain I: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 202-209 | 8 | |
| α-helix | 210-214 | 5 | |
| α-helix | 226-271 | 46 | |
Chain J: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 89-149 | 61 | |
Chain K: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-283 | 219 | |
Chain L: 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 | protein | 377 | Mus musculus | P68033 (AlphaFold model) |
| Troponin C, slow skeletal and cardiac muscles | G | protein | 161 | Mus musculus | P19123 (AlphaFold model) |
| Troponin I, cardiac muscle | H | protein | 211 | Mus musculus | P48787 (AlphaFold model) |
| Isoform 6 of Troponin T, cardiac muscle | I, J | protein | 288 | Mus musculus | P45379 (AlphaFold model) |
| Tropomyosin alpha-1 chain | K, L, M, N | protein | 284 | Mus musculus | P58771 |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>9MO9_1 Actin, alpha cardiac muscle 1 (chains A, B, C, D, E, F)
MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
LSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIS
KQEYDEAGPSIVHRKCF
Sequence of entity 2 (G), FASTA
>9MO9_2 Troponin C, slow skeletal and cardiac muscles (chains G)
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEM
IDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKMM
LQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Sequence of entity 3 (H), FASTA
>9MO9_3 Troponin I, cardiac muscle (chains H)
MADESSDAAGEPQPAPAPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQ
EMEREAEERRGEKGRVLRTRCQPLELDGLGFEELQDLCRQLHARVDKVDEERYDVEAKVT
KNITEIADLTQKIYDLRGKFKRPTLRRVRISADAMMQALLGTRAKESLDLRAHLKQVKKE
DIEKENREVGDWRKNIDALSGMEGRKKKFEG
Sequence of entity 4 (I, J), FASTA
>9MO9_4 Isoform 6 of Troponin T, cardiac muscle (chains I, J)
MSDIEEVVEEYEEEEQEEAAVEEQEEAAEEDAEAEAETEETRAEEDEEEEEAKEAEDGPM
EESKPKPRSFMPNLVPPKNPDGERVDFDDIHRKRMEKDLNELQALIEAHFENRKKEEEEL
VSLKDRIERRRAERAEQQRIRNEREKERQNRLAEERARREEEENRRKAEDEARKKKALSN
MMHFGGYIQKQAQTERKSGKRQTEREKKKKILAERRKVLAIDHLNEDQLREKAKELWQSI
YNLEAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK
Sequence of entity 5 (K, L, M, N), FASTA
>9MO9_5 Tropomyosin alpha-1 chain (chains K, L, M, N)
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKY
SEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA
DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE
ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE
FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 6 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 6 |
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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