Structure of the actin-depolymerizing factor homology domain in complex with actin. Determined by X-ray diffraction at 2.55 Å resolution. Released 29 Jul 2008.
Explore 3DAW in 3D Show helices and sheets RCSB PDB PDBe
3DAW contains 28 α-helices and 27 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 | 22 | 1 | 2 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 3 |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 55-60 | 6 | |
| β-strand | 65-68 | 4 | 3 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| 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 | 5 |
| β-strand | 160-166 | 7 | 5 |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 182-195 | 14 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 338-347 | 10 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-363 | 5 | |
| α-helix | 370-374 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 180-181 | 2 | |
| β-strand | 182 | 1 | 7 |
| α-helix | 183 | 1 | |
| α-helix | 184-194 | 11 | |
| β-strand | 200-206 | 7 | 7 |
| β-strand | 211-216 | 6 | 7 |
| α-helix | 222-224 | 3 | |
| α-helix | 226-228 | 3 | |
| β-strand | 235-245 | 11 | 7 |
| β-strand | 248-258 | 11 | 7 |
| α-helix | 266-274 | 9 | |
| α-helix | 276-287 | 12 | |
| β-strand | 291-297 | 7 | 7 |
| α-helix | 305-312 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A | protein | 377 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Twinfilin-1 | B | protein | 164 | Mus musculus | Q91YR1 (AlphaFold model) |
>3DAW_1 Actin, alpha skeletal muscle (chains A) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVHRKCF
>3DAW_2 Twinfilin-1 (chains B) MSHHHHHHSMDTKHQTLQGVAFPISRDAFQALEKLSKKQLNYVQLEIDIKNETIILANTE NTELRDLPKRIPKDSARYHFFLYKHSHEGDYLESVVFIYSMPGYTCSIRERMLYSSCKSP LLEIVERQLQMDVIRKIEIDNGDELTADFLYDEVHPKQHAHKQS
Structure of the actin-depolymerizing factor homology domain in complex with actin. Paavilainen, V.O., Oksanen, E., Goldman, A. et al. J Cell Biol (2008) 182:51-59. DOI 10.1083/jcb.200803100 · 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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