Acanthamoeba Actin complex with Spir domain D. Determined by X-ray diffraction at 2.48 Å resolution. Released 11 Apr 2012.
Explore 4EFH in 3D Show helices and sheets RCSB PDB PDBe
4EFH contains 24 α-helices and 19 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 | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 3 |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 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 | 182-193 | 12 | |
| α-helix | 194-196 | 3 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 5 |
| β-strand | 247-250 | 4 | 5 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 338-347 | 10 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 76-86 | 11 | |
| β-strand | 91 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin-1 | A | protein | 375 | Acanthamoeba castellanii | P02578 (AlphaFold model) |
| Protein spire | B | protein | 66 | Drosophila melanogaster | Q9U1K1 (AlphaFold model) |
>4EFH_1 Actin-1 (chains A) MGDEVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDL AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMHTAASSSALEKSY ELPDGQVITIGNERFRAPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLS GGTTMFPGIADRMQKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKE EYDESGPSIVHRKCF
>4EFH_2 Protein spire (chains B) GPLGSKKDAHAMILEFIRSRPPLKKASDRQLGPPRMCEPSPREQLMESIRKGKELKQITP PEAAAS
Multiple Forms of Spire-Actin Complexes and their Functional Consequences. Chen, C.K., Sawaya, M.R., Phillips, M.L. et al. J Biol Chem (2012) 287:10684-10692. DOI 10.1074/jbc.M111.317792 · PubMed
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