CARP domain of mouse cyclase-associated protein 1 (CAP1) bound to ADP-actin. Determined by X-ray diffraction at 2.8 Å resolution. Released 16 May 2018.
Explore 6FM2 in 3D Show helices and sheets RCSB PDB PDBe
6FM2 contains 28 α-helices and 36 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 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 | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 2 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| α-helix | 127 | 1 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 3 |
| β-strand | 160-166 | 7 | 3 |
| β-strand | 169-170 | 2 | 3 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 3 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 4 |
| β-strand | 247-250 | 4 | 4 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-260 | 3 | |
| α-helix | 264-266 | 3 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-284 | 11 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 3 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 3 |
| α-helix | 333-337 | 5 | |
| α-helix | 338-348 | 11 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-368 | 3 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 320-324 | 5 | 5 |
| β-strand | 327-331 | 5 | 5 |
| β-strand | 334 | 1 | 6 |
| β-strand | 339-341 | 3 | 6 |
| β-strand | 349-353 | 5 | 5 |
| β-strand | 356 | 1 | 6 |
| β-strand | 359-366 | 8 | 6 |
| β-strand | 369-372 | 4 | 5 |
| β-strand | 375 | 1 | 6 |
| β-strand | 378-384 | 7 | 6 |
| β-strand | 387-391 | 5 | 5 |
| β-strand | 394-400 | 7 | 6 |
| β-strand | 406-410 | 5 | 5 |
| β-strand | 413-418 | 6 | 6 |
| α-helix | 423-425 | 3 | |
| β-strand | 427-431 | 5 | 5 |
| β-strand | 434-441 | 8 | 6 |
| β-strand | 447-451 | 5 | 6 |
| α-helix | 452-453 | 2 | |
| β-strand | 456-460 | 5 | 7 |
| β-strand | 465-469 | 5 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A | protein | 375 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Adenylyl cyclase-associated protein 1 | B | protein | 158 | Mus musculus | P40124 (AlphaFold model) |
>6FM2_1 Actin, alpha skeletal muscle (chains A) DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ EYDEAGPSIVHRKCF
>6FM2_2 Adenylyl cyclase-associated protein 1 (chains B) EPALLELEGKKWRVENQENVSNLVIDDTELKQVAYIYKCVNTTLQIKGKINSITVDNCKK LGLVFDDVVGIVEIINSRDVKVQVMGKVPTISINKTDGCHAYLSKNSLDCEIVSAKSSEM NVLIPTEGGDFNEFPVPEQFKTLWNGQKLVTTVTEIAG
Structural basis of actin monomer re-charging by cyclase-associated protein. Kotila, T., Kogan, K., Enkavi, G. et al. Nat Commun (2018) 9:1892-1892. DOI 10.1038/s41467-018-04231-7 · PubMed
Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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