HFD domain of mouse CAP1 bound to the pointed end of G-actin. Determined by X-ray diffraction at 1.95 Å resolution. Released 27 Nov 2019.
Explore 6RSW in 3D Show helices and sheets RCSB PDB PDBe
6RSW contains 39 α-helices and 25 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| 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 | |
| α-helix | 62-64 | 3 | |
| 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 | 89-94 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 4 |
| β-strand | 160-166 | 7 | 4 |
| β-strand | 169-170 | 2 | 4 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 182-196 | 15 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 5 |
| β-strand | 247-250 | 4 | 5 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-284 | 11 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 338-348 | 11 | |
| α-helix | 350-354 | 5 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-372 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 180-181 | 2 | |
| β-strand | 182 | 1 | 6 |
| α-helix | 183 | 1 | |
| α-helix | 184-194 | 11 | |
| β-strand | 200-206 | 7 | 6 |
| β-strand | 211-216 | 6 | 6 |
| α-helix | 222-228 | 7 | |
| β-strand | 235-245 | 11 | 6 |
| β-strand | 248-258 | 11 | 6 |
| α-helix | 266-287 | 22 | |
| β-strand | 291-297 | 7 | 6 |
| α-helix | 300-302 | 3 | |
| α-helix | 305-312 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-49 | 9 | |
| α-helix | 50-54 | 5 | |
| α-helix | 55-64 | 10 | |
| α-helix | 66-90 | 25 | |
| α-helix | 97-119 | 23 | |
| α-helix | 127-134 | 8 | |
| α-helix | 137-144 | 8 | |
| α-helix | 149-171 | 23 | |
| α-helix | 176-199 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A | protein | 375 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Twinfilin-1 | B | protein | 141 | Mus musculus | Q91YR1 (AlphaFold model) |
| Adenylyl cyclase-associated protein 1 | C | protein | 172 | Mus musculus | P40124 (AlphaFold model) |
>6RSW_1 Actin, alpha skeletal muscle (chains A) DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ EYDEAGPSIVHRKCF
>6RSW_2 Twinfilin-1 (chains B) QGVAFPISRDAFQALEKLSKKQLNYVQLEIDIKNETIILANTENTELRDLPKRIPKDSAR YHFFLYKHSHEGDYLESVVFIYSMPGYTCSIRERMLYSSCKSPLLEIVERQLQMDVIRKI EIDNGDELTADFLYDEVHPKQ
>6RSW_3 Adenylyl cyclase-associated protein 1 (chains C) AVPYVQAFDSLLANPVAEYLKMSKEIGGDVQKHAEMVHTGLKLERALLATASQSQQPAGN KLSDLLAPISEQIQEVITFREKNRGSKFFNHLSAVSESIQALGWVALAAKPGPFVKEMND AAMFYTNRVLKEYRDVDKKHVDWVRAYLSIWTELQAYIKEFHTTGLAWSKTG
Water and common crystallization additives (EPE) are not listed.
Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin. Kotila, T., Wioland, H., Enkavi, G. et al. Nat Commun (2019) 10:5320-5320. DOI 10.1038/s41467-019-13213-2 · 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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