8UWW: Actin, alpha cardiac muscle 1
The structure of the native cardiac thin filament troponin core in Ca2+-free state from the upper strand. Determined by electron microscopy at 5.1 Å resolution. Released 6 Mar 2024.
- Method
- Electron microscopy
- Resolution
- 5.1 Å
- Organism
- Sus scrofa
- Chains
- 7
- Atoms
- 10,176
- Mol. weight
- 226.12 kDa
- Released
- 6 Mar 2024
Explore 8UWW in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8UWW contains 61 α-helices and 46 β-strands across 7 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: 22 helices, 22 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 | 24 | 1 | 3 |
| β-strand | 29-31 | 3 | 2 |
| β-strand | 35-38 | 4 | 4 |
| β-strand | 53-54 | 2 | 4 |
| α-helix | 55-59 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 4 |
| β-strand | 71 | 1 | 5 |
| β-strand | 76 | 1 | 5 |
| 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 | 6 |
| β-strand | 160-166 | 7 | 6 |
| β-strand | 169-170 | 2 | 6 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 6 |
| 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 | 7 |
| β-strand | 245-250 | 6 | 7 |
| α-helix | 258-261 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 6 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 6 |
| 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 B: 22 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8 | 1 | 8 |
| β-strand | 11 | 1 | 9 |
| β-strand | 17-19 | 3 | 9 |
| β-strand | 21 | 1 | 8 |
| β-strand | 29-31 | 3 | 9 |
| β-strand | 35-38 | 4 | 10 |
| β-strand | 53-54 | 2 | 10 |
| α-helix | 55-59 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 10 |
| β-strand | 71 | 1 | 11 |
| β-strand | 76 | 1 | 11 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-94 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 8 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 8 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 12 |
| β-strand | 160-166 | 7 | 12 |
| β-strand | 169-170 | 2 | 12 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 12 |
| 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 | 13 |
| β-strand | 245-250 | 6 | 13 |
| α-helix | 258-261 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 12 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 12 |
| α-helix | 338-347 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 8 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-369 | 3 | |
Chain C: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-9 | 6 | |
| α-helix | 14-24 | 11 | |
| α-helix | 41-44 | 4 | |
| α-helix | 54-63 | 10 | |
| α-helix | 74-82 | 9 | |
| α-helix | 94-104 | 11 | |
| β-strand | 112 | 1 | 14 |
| α-helix | 114-123 | 10 | |
| α-helix | 134-140 | 7 | |
| β-strand | 148 | 1 | 14 |
| α-helix | 150-156 | 7 | |
Chain D: 4 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-80 | 36 | |
| α-helix | 91-141 | 51 | |
| α-helix | 142-144 | 3 | |
| β-strand | 147 | 1 | 3 |
| α-helix | 158-171 | 14 | |
Chain E: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 200-212 | 13 | |
| α-helix | 223-266 | 44 | |
Chains F and G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 135-214 | 80 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Actin, alpha cardiac muscle 1 | A, B | protein | 377 | Sus scrofa | A0A8W4F696 (AlphaFold model) |
| Troponin C, slow skeletal and cardiac muscles | C | protein | 161 | Sus scrofa | P63317 (AlphaFold model) |
| Troponin I, cardiac muscle | D | protein | 211 | Sus scrofa | A0A4X1V520 (AlphaFold model) |
| Troponin T2, cardiac type | E | protein | 285 | Sus scrofa | A0A5G2Q8N0 (AlphaFold model) |
| Tropomyosin alpha-1 chain | F, G | protein | 284 | Sus scrofa | P42639 |
Sequence of entity 1 (A, B), FASTA
>8UWW_1 Actin, alpha cardiac muscle 1 (chains A, B)
MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
LSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIS
KQEYDEAGPSIVHRKCF
Sequence of entity 2 (C), FASTA
>8UWW_2 Troponin C, slow skeletal and cardiac muscles (chains C)
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEM
IDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLEELKIM
LQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Sequence of entity 3 (D), FASTA
>8UWW_3 Troponin I, cardiac muscle (chains D)
MADRSGDAAGDSRPAPAPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQ
ELEREAEERRGEKGRALSTRCQPLELAGLSFAELQDLCRQLHARVDKVDEERYDVEAKVT
KNITEIADLNQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKETLDLRAHLKQVKKE
DTEKENREVGDWRKNIDALSGMEGRKKKFEG
Sequence of entity 4 (E), FASTA
>8UWW_4 Troponin T2, cardiac type (chains E)
MSDVEETVDEYEEEQEEGAAEEQEEAVEEEAGGEAEAEEANAEEAGQEEDGREAEDGPME
ESKPKPRLFMPNLVPPKIPDGERVDFDDIHRKRMKDLNELQTLIEAHFENRKKEEELVSL
KDRIEKRRAERAEQQRIRTEREKERQTRLAEERARREEEENRRKAEDEARKKKALSNMMH
FGGYIQKQAQTERKSGKRQTEREKKKKILAERRKVLAIDHLNEDQLREKAKELWQSIYNL
EAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK
Sequence of entity 5 (F, G), FASTA
>8UWW_5 Tropomyosin alpha-1 chain (chains F, G)
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKRLEDELVSLQKKLKATEDELDKY
SEAPKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA
DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE
ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE
FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Primary citation
Troponin Structural Dynamics in the Native Cardiac Thin Filament Revealed by Cryo Electron Microscopy. Risi, C.M., Belknap, B., Atherton, J. et al. J Mol Biol (2024) 436:168498-168498. DOI 10.1016/j.jmb.2024.168498 · PubMed
Other PDB entries of the same protein (UniProt A0A8W4F696 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9BPM 3.42 Å, cryo-EM structure of cardiac muscle alpha-actin A331P hcm mutant
- 8V0K 5.2 Å, The structure of the native cardiac thin filament troponin core in Ca2+-bound partially…
- 8UYD 5.3 Å, The structure of the native cardiac thin filament troponin core in Ca2+-free state from…
- 8UZY 5.3 Å, The structure of the native cardiac thin filament troponin core in Ca2+-bound partially…
- 8UZX 5.4 Å, The structure of the native cardiac thin filament troponin core in Ca2+-bound fully…
- 8UWY 5.5 Å, The structure of the native cardiac thin filament troponin core in Ca2+-free rotated…
- 8V01 5.5 Å, The structure of the native cardiac thin filament troponin core in Ca2+-bound fully…
- 8V0I 5.8 Å, The structure of the native cardiac thin filament troponin core in Ca2+-bound fully…
- 8UZ5 5.9 Å, The structure of the native cardiac thin filament troponin core in Ca2+-free rotated…
- 8UWX 6.0 Å, The structure of the native cardiac thin filament troponin core in Ca2+-free tilted…
- 8V0Y 7.0 Å, The structure of the native cardiac thin filament troponin core in Ca2+-free state from…
- 8UZ6 7.1 Å, The structure of the native cardiac thin filament troponin core in Ca2+-free tilted…
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