7UTI: Actin, alpha skeletal muscle
Alternative modeling of tropomyosin in human cardiac thin filament in the calcium bound state. Determined by electron microscopy at 4.8 Å resolution. Released 21 Sept 2022.
- Method
- Electron microscopy
- Resolution
- 4.8 Å
- Organisms
- Oryctolagus cuniculus, Homo sapiens
- Chains
- 32
- Atoms
- 64,508
- Mol. weight
- 1167.14 kDa
- Ligands
- CA, MG, ADP
- Released
- 21 Sept 2022
Explore 7UTI in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7UTI contains 376 α-helices and 295 β-strands across 32 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 and V: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 43-79 | 37 | |
| α-helix | 90-136 | 47 | |
| α-helix | 151-159 | 9 | |
Chains b and W: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-51 | 50 | |
Chains c and X: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 90-149 | 60 | |
Chains C, E, F, H, O and P: 21 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-13 | 6 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-59 | 4 | |
| β-strand | 65-68 | 4 | 2 |
| β-strand | 71-72 | 2 | 3 |
| β-strand | 75-76 | 2 | 3 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 4 |
| β-strand | 160-165 | 6 | 4 |
| β-strand | 170 | 1 | 4 |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 182-196 | 15 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 5 |
| β-strand | 247-250 | 4 | 5 |
| α-helix | 253-256 | 4 | |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-284 | 11 | |
| α-helix | 287-295 | 9 | |
| β-strand | 298-300 | 3 | 4 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| α-helix | 335-347 | 13 | |
| α-helix | 350-354 | 5 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-374 | 8 | |
Chains d and Y: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 200-215 | 16 | |
| α-helix | 226-268 | 43 | |
Chain D: 21 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-13 | 6 | 6 |
| β-strand | 16-21 | 6 | 6 |
| β-strand | 29-32 | 4 | 6 |
| β-strand | 35-38 | 4 | 7 |
| β-strand | 53-54 | 2 | 7 |
| α-helix | 56-59 | 4 | |
| β-strand | 65-68 | 4 | 7 |
| β-strand | 71-72 | 2 | 8 |
| β-strand | 75-76 | 2 | 8 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| β-strand | 103-107 | 5 | 6 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 6 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 9 |
| β-strand | 160-165 | 6 | 9 |
| β-strand | 166 | 1 | 10 |
| β-strand | 169 | 1 | 10 |
| β-strand | 176-178 | 3 | 9 |
| α-helix | 182-196 | 15 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 11 |
| β-strand | 247-250 | 4 | 11 |
| α-helix | 253-256 | 4 | |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-284 | 11 | |
| α-helix | 287-295 | 9 | |
| β-strand | 298-300 | 3 | 9 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| α-helix | 335-347 | 13 | |
| α-helix | 350-354 | 5 | |
| β-strand | 357-358 | 2 | 6 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-374 | 8 | |
Chain e: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-282 | 264 | |
Chain f: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-283 | 265 | |
7 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 skeletal muscle | C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R | protein | 377 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Tropomyosin alpha-1 chain | W, b, e, f, g, h, i, j | protein | 285 | Homo sapiens | P09493 (AlphaFold model) |
| Isoform 6 of Troponin T, cardiac muscle | X, Y, c, d | protein | 288 | Homo sapiens | P45379 (AlphaFold model) |
| Troponin I, cardiac muscle | V, a | protein | 210 | Homo sapiens | P19429 (AlphaFold model) |
| Troponin C, slow skeletal and cardiac muscles | U, Z | protein | 161 | Homo sapiens | P63316 |
Sequence of entity 1 (C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R), FASTA
>7UTI_1 Actin, alpha skeletal muscle (chains C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF
Sequence of entity 2 (W, b, e, f, g, h, i, j), FASTA
>7UTI_2 Tropomyosin alpha-1 chain (chains W, b, e, f, g, h, i, j)
XMDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDK
YSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA
ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERA
EERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRA
EFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Sequence of entity 3 (X, Y, c, d), FASTA
>7UTI_3 Isoform 6 of Troponin T, cardiac muscle (chains X, Y, c, d)
MSDIEEVVEEYEEEEQEEAAVEEQEEAAEEDAEAEAETEETRAEEDEEEEEAKEAEDGPM
EESKPKPRSFMPNLVPPKIPDGERVDFDDIHRKRMEKDLNELQALIEAHFENRKKEEEEL
VSLKDRIERRRAERAEQQRIRNEREKERQNRLAEERARREEEENRRKAEDEARKKKALSN
MMHFGGYIQKQAQTERKSGKRQTEREKKKKILAERRKVLAIDHLNEDQLREKAKELWQSI
YNLEAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK
Sequence of entity 4 (V, a), FASTA
>7UTI_4 Troponin I, cardiac muscle (chains V, a)
MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQIAKQE
LEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEERYDIEAKVTK
NITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKED
TEKENREVGDWRKNIDALSGMEGRKKKFES
Sequence of entity 5 (U, Z), FASTA
>7UTI_5 Troponin C, slow skeletal and cardiac muscles (chains U, Z)
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEM
IDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIM
LQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 6 |
| MG | Magnesium ion | Mg | 16 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 16 |
Primary citation
Protein-Protein Docking Reveals Dynamic Interactions of Tropomyosin on Actin Filaments. Pavadai, E., Lehman, W., Rynkiewicz, M.J. Biophys J (2020) 119:75-86. DOI 10.1016/j.bpj.2020.05.017 · PubMed
Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4B1Y 1.29 Å, Structure of the Phactr1 RPEL-3 bound to G-actin
- 2FXU 1.35 Å, X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
- 4K41 1.4 Å, Crystal structure of actin in complex with marine macrolide kabiramide C
- 1QZ5 1.45 Å, Structure of rabbit actin in complex with kabiramide C
- 1WUA 1.45 Å, The structure of Aplyronine A-actin complex
- 2Q0U 1.45 Å, Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin
- 2V52 1.45 Å, Structure of MAL-RPEL2 complexed to G-actin
- 3MN5 1.5 Å, Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation
- 2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
- 5ZZA 1.53 Å, OdinProfilin/Rabbit Actin Complex
- 1J6Z 1.54 Å, Uncomplexed actin
- 1QZ6 1.6 Å, Structure of rabbit actin in complex with jaspisamide A
Browse structure collections
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