6G2T: Actin, cytoplasmic 2
human cardiac myosin binding protein C C1 Ig-domain bound to native cardiac thin filament. Determined by electron microscopy at 9.0 Å resolution. Released 17 Oct 2018.
- Method
- Electron microscopy
- Resolution
- 9.0 Å
- Organisms
- Homo sapiens, Sus scrofa
- Chains
- 16
- Atoms
- 24,958
- Mol. weight
- 370.15 kDa
- Released
- 17 Oct 2018
Explore 6G2T in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6G2T contains 140 α-helices and 170 β-strands across 16 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: 20 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-12 | 6 | 1 |
| β-strand | 15-20 | 6 | 1 |
| β-strand | 28-31 | 4 | 1 |
| β-strand | 34-37 | 4 | 2 |
| α-helix | 40-41 | 2 | |
| β-strand | 52-53 | 2 | 2 |
| α-helix | 55-59 | 5 | |
| β-strand | 64-67 | 4 | 2 |
| β-strand | 70-71 | 2 | 3 |
| β-strand | 74-75 | 2 | 3 |
| α-helix | 78-86 | 9 | |
| α-helix | 87-93 | 7 | |
| β-strand | 102-106 | 5 | 1 |
| α-helix | 112-125 | 14 | |
| β-strand | 130-135 | 6 | 1 |
| α-helix | 136-144 | 9 | |
| β-strand | 149-153 | 5 | 4 |
| β-strand | 159-165 | 7 | 4 |
| β-strand | 168-169 | 2 | 4 |
| β-strand | 175-177 | 3 | 4 |
| α-helix | 181-195 | 15 | |
| α-helix | 202-214 | 13 | |
| α-helix | 222-227 | 6 | |
| α-helix | 228-231 | 4 | |
| β-strand | 237-240 | 4 | 5 |
| β-strand | 246-249 | 4 | 5 |
| α-helix | 252-261 | 10 | |
| α-helix | 271-272 | 2 | |
| α-helix | 273-283 | 11 | |
| α-helix | 286-294 | 9 | |
| β-strand | 296-299 | 4 | 4 |
| α-helix | 301-304 | 4 | |
| α-helix | 308-319 | 12 | |
| β-strand | 328-329 | 2 | 4 |
| α-helix | 337-347 | 11 | |
| α-helix | 349-353 | 5 | |
| β-strand | 356-357 | 2 | 1 |
| α-helix | 358-364 | 7 | |
| α-helix | 368-372 | 5 | |
Chain B: 20 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-11 | 5 | 6 |
| β-strand | 15-20 | 6 | 6 |
| β-strand | 28-31 | 4 | 6 |
| β-strand | 34-37 | 4 | 7 |
| β-strand | 52-53 | 2 | 7 |
| α-helix | 55-59 | 5 | |
| β-strand | 64-67 | 4 | 7 |
| β-strand | 70-71 | 2 | 8 |
| β-strand | 74-75 | 2 | 8 |
| α-helix | 78-86 | 9 | |
| α-helix | 87-93 | 7 | |
| β-strand | 102-106 | 5 | 6 |
| α-helix | 112-124 | 13 | |
| β-strand | 130-135 | 6 | 6 |
| α-helix | 136-144 | 9 | |
| β-strand | 149-153 | 5 | 9 |
| β-strand | 159-164 | 6 | 9 |
| β-strand | 165 | 1 | 10 |
| β-strand | 168 | 1 | 10 |
| β-strand | 175-177 | 3 | 9 |
| α-helix | 181-194 | 14 | |
| α-helix | 202-215 | 14 | |
| α-helix | 222-227 | 6 | |
| α-helix | 228-231 | 4 | |
| β-strand | 237-240 | 4 | 11 |
| β-strand | 246-249 | 4 | 11 |
| α-helix | 252-261 | 10 | |
| α-helix | 263-266 | 4 | |
| α-helix | 273-283 | 11 | |
| α-helix | 286-294 | 9 | |
| β-strand | 296-299 | 4 | 9 |
| α-helix | 301-303 | 3 | |
| α-helix | 308-319 | 12 | |
| β-strand | 328-329 | 2 | 9 |
| α-helix | 334-336 | 3 | |
| α-helix | 337-347 | 11 | |
| α-helix | 349-354 | 6 | |
| β-strand | 356-357 | 2 | 6 |
| α-helix | 358-364 | 7 | |
| α-helix | 368-372 | 5 | |
Chain C: 22 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-12 | 6 | 12 |
| β-strand | 15-20 | 6 | 12 |
| β-strand | 28-31 | 4 | 12 |
| β-strand | 34-37 | 4 | 13 |
| α-helix | 40-41 | 2 | |
| β-strand | 52-53 | 2 | 13 |
| α-helix | 55-59 | 5 | |
| β-strand | 64-67 | 4 | 13 |
| β-strand | 70-71 | 2 | 14 |
| β-strand | 74-75 | 2 | 14 |
| α-helix | 78-86 | 9 | |
| α-helix | 87-93 | 7 | |
| β-strand | 102-106 | 5 | 12 |
| α-helix | 112-124 | 13 | |
| β-strand | 130-135 | 6 | 12 |
| α-helix | 136-144 | 9 | |
| β-strand | 149-154 | 6 | 15 |
| β-strand | 159-165 | 7 | 15 |
| β-strand | 168-169 | 2 | 15 |
| β-strand | 175-177 | 3 | 15 |
| α-helix | 181-195 | 15 | |
| α-helix | 202-214 | 13 | |
| α-helix | 222-227 | 6 | |
| α-helix | 228-230 | 3 | |
| β-strand | 237-240 | 4 | 16 |
| β-strand | 246-249 | 4 | 16 |
| α-helix | 251-261 | 11 | |
| α-helix | 263-266 | 4 | |
| α-helix | 271-272 | 2 | |
| α-helix | 273-283 | 11 | |
| α-helix | 286-294 | 9 | |
| β-strand | 296-299 | 4 | 15 |
| α-helix | 301-303 | 3 | |
| α-helix | 308-319 | 12 | |
| β-strand | 328-329 | 2 | 15 |
| α-helix | 334-336 | 3 | |
| α-helix | 337-347 | 11 | |
| α-helix | 349-354 | 6 | |
| β-strand | 356-357 | 2 | 12 |
| α-helix | 358-364 | 7 | |
| α-helix | 368-372 | 5 | |
Chain D: 20 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-11 | 5 | 17 |
| β-strand | 15-20 | 6 | 17 |
| β-strand | 28-31 | 4 | 17 |
| β-strand | 34-37 | 4 | 18 |
| β-strand | 41 | 1 | 19 |
| β-strand | 52-53 | 2 | 18 |
| α-helix | 55-59 | 5 | |
| β-strand | 64-67 | 4 | 18 |
| β-strand | 70-71 | 2 | 20 |
| β-strand | 74-75 | 2 | 20 |
| α-helix | 78-86 | 9 | |
| α-helix | 87-93 | 7 | |
| β-strand | 102-106 | 5 | 17 |
| α-helix | 112-124 | 13 | |
| β-strand | 130-135 | 6 | 17 |
| α-helix | 136-144 | 9 | |
| β-strand | 149-153 | 5 | 21 |
| β-strand | 159-165 | 7 | 21 |
| β-strand | 168-169 | 2 | 21 |
| β-strand | 175-177 | 3 | 21 |
| α-helix | 181-195 | 15 | |
| α-helix | 202-214 | 13 | |
| α-helix | 222-227 | 6 | |
| α-helix | 228-230 | 3 | |
| β-strand | 237-240 | 4 | 22 |
| β-strand | 246-249 | 4 | 22 |
| α-helix | 251-261 | 11 | |
| α-helix | 263-266 | 4 | |
| α-helix | 273-283 | 11 | |
| α-helix | 286-294 | 9 | |
| β-strand | 296-299 | 4 | 21 |
| α-helix | 302-304 | 3 | |
| α-helix | 308-319 | 12 | |
| β-strand | 328-329 | 2 | 21 |
| α-helix | 334-336 | 3 | |
| α-helix | 337-345 | 9 | |
| α-helix | 349-354 | 6 | |
| β-strand | 356-357 | 2 | 17 |
| α-helix | 358-364 | 7 | |
| α-helix | 368-372 | 5 | |
Chain E: 19 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-11 | 5 | 23 |
| β-strand | 15-20 | 6 | 23 |
| β-strand | 28-31 | 4 | 23 |
| β-strand | 34-37 | 4 | 24 |
| β-strand | 52-53 | 2 | 24 |
| α-helix | 55-59 | 5 | |
| β-strand | 64-67 | 4 | 24 |
| β-strand | 70-71 | 2 | 25 |
| β-strand | 74-75 | 2 | 25 |
| α-helix | 78-86 | 9 | |
| α-helix | 87-93 | 7 | |
| β-strand | 102-106 | 5 | 23 |
| α-helix | 112-124 | 13 | |
| β-strand | 130-135 | 6 | 23 |
| α-helix | 136-144 | 9 | |
| β-strand | 149-153 | 5 | 26 |
| β-strand | 159-165 | 7 | 26 |
| β-strand | 168-169 | 2 | 26 |
| β-strand | 175-177 | 3 | 26 |
| α-helix | 181-195 | 15 | |
| α-helix | 202-215 | 14 | |
| α-helix | 222-228 | 7 | |
| β-strand | 237-240 | 4 | 27 |
| β-strand | 246-249 | 4 | 27 |
| α-helix | 252-261 | 10 | |
| α-helix | 271-272 | 2 | |
| α-helix | 273-283 | 11 | |
| α-helix | 286-294 | 9 | |
| β-strand | 296-299 | 4 | 26 |
| α-helix | 301-304 | 4 | |
| α-helix | 308-319 | 12 | |
| β-strand | 328-329 | 2 | 26 |
| α-helix | 334-336 | 3 | |
| α-helix | 337-347 | 11 | |
| α-helix | 349-354 | 6 | |
| β-strand | 356-357 | 2 | 23 |
| α-helix | 358-364 | 7 | |
| α-helix | 368-372 | 5 | |
Chain F: 19 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-11 | 5 | 28 |
| β-strand | 15-20 | 6 | 28 |
| β-strand | 28-31 | 4 | 28 |
| β-strand | 34-37 | 4 | 29 |
| β-strand | 52-53 | 2 | 29 |
| α-helix | 55-59 | 5 | |
| β-strand | 64-67 | 4 | 29 |
| β-strand | 70-71 | 2 | 30 |
| β-strand | 74-75 | 2 | 30 |
| α-helix | 78-86 | 9 | |
| α-helix | 87-93 | 7 | |
| β-strand | 102-106 | 5 | 28 |
| α-helix | 112-124 | 13 | |
| β-strand | 130-135 | 6 | 28 |
| α-helix | 136-144 | 9 | |
| β-strand | 149-154 | 6 | 19 |
| β-strand | 159-165 | 7 | 19 |
| β-strand | 168-169 | 2 | 19 |
| β-strand | 175-177 | 3 | 19 |
| α-helix | 181-195 | 15 | |
| α-helix | 202-215 | 14 | |
| α-helix | 222-227 | 6 | |
| α-helix | 228-231 | 4 | |
| β-strand | 237-240 | 4 | 31 |
| β-strand | 246-249 | 4 | 31 |
| α-helix | 252-261 | 10 | |
| α-helix | 271-272 | 2 | |
| α-helix | 273-283 | 11 | |
| α-helix | 286-294 | 9 | |
| β-strand | 296-299 | 4 | 19 |
| α-helix | 308-319 | 12 | |
| β-strand | 328-329 | 2 | 19 |
| α-helix | 334-336 | 3 | |
| α-helix | 337-347 | 11 | |
| α-helix | 349-354 | 6 | |
| β-strand | 356-357 | 2 | 28 |
| α-helix | 358-364 | 7 | |
| α-helix | 368-372 | 5 | |
Chains G, H and K: 2 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 157-159 | 3 | 32 |
| β-strand | 164-167 | 4 | 33 |
| β-strand | 172-179 | 8 | 32 |
| β-strand | 188-193 | 6 | 33 |
| β-strand | 197-198 | 2 | 33 |
| α-helix | 199-202 | 4 | |
| β-strand | 207-214 | 8 | 32 |
| β-strand | 219-226 | 8 | 32 |
| α-helix | 231-233 | 3 | |
| β-strand | 235-242 | 8 | 33 |
| β-strand | 247-257 | 11 | 33 |
Chain I: 2 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 159 | 1 | 36 |
| β-strand | 164-167 | 4 | 37 |
| β-strand | 172-179 | 8 | 36 |
| β-strand | 188-193 | 6 | 37 |
| β-strand | 197-198 | 2 | 37 |
| α-helix | 199-202 | 4 | |
| β-strand | 207-214 | 8 | 36 |
| β-strand | 219-226 | 8 | 36 |
| α-helix | 231-233 | 3 | |
| β-strand | 235-242 | 8 | 37 |
| β-strand | 247-257 | 11 | 37 |
6 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, cytoplasmic 2 | A, B, C, D, E, F | protein | 375 | Homo sapiens | P63261 (AlphaFold model) |
| Myosin-binding protein C, cardiac-type | G, H, I, J, K, L | protein | 109 | Homo sapiens | Q14896 (AlphaFold model) |
| Tropomyosin | M, N, O, P | protein | 135 | Sus scrofa | |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>6G2T_1 Actin, cytoplasmic 2 (chains A, B, C, D, E, F)
MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT
QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL
AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ
EYDESGPSIVHRKCF
Sequence of entity 2 (G, H, I, J, K, L), FASTA
>6G2T_2 Myosin-binding protein C, cardiac-type (chains G, H, I, J, K, L)
MDDPIGLFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQL
HDSYDRASKVYLFELHITDAQPAFTGSYRCEVSTKDKFDCSNFNLTVHE
Sequence of entity 3 (M, N, O, P), FASTA
>6G2T_3 Tropomyosin (chains M, N, O, P)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXX
Primary citation
N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament. Risi, C., Belknap, B., Forgacs-Lonart, E. et al. Structure (2018) 26:1604-1611.e4. DOI 10.1016/j.str.2018.08.007 · PubMed
Other PDB entries of the same protein (UniProt P63261 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6WK2 1.76 Å, SETD3 mutant (N255V) in Complex with an Actin Peptide with His73 Replaced with Methionine
- 6WK1 1.89 Å, SETD3 in Complex with an Actin Peptide with His73 Replaced with Methionine
- 6V63 2.02 Å, SETD3 WT in Complex with an Actin Peptide with His73 Replaced with Glutamine
- 6V62 2.36 Å, SETD3 double mutant (N255F/W273A) in Complex with an Actin Peptide with His73 Replaced…
- 7NVM 3.1 Å, Human TRiC complex in closed state with nanobody Nb18, actin and PhLP2A bound
- 8DNF 3.38 Å, Cryo-EM structure of nonmuscle gamma-actin
- 9SMX 3.67 Å, CM1-activated gTuRC in complex with nascent alpha-E254D mutant microtubules
- 5JLH 3.9 Å, Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution
- 6CXI 11.0 Å, Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C…
- 6CXJ 11.0 Å, Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C…
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