Structure of the Phactr1 RPEL-2 domain bound to actin. Determined by X-ray diffraction at 1.95 Å resolution. Released 31 Jul 2013.
Explore 4B1W in 3D Show helices and sheets RCSB PDB PDBe
4B1W contains 25 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 | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-59 | 4 | |
| 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 | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| 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 | 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 | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 338-347 | 10 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 422-429 | 8 | |
| α-helix | 434-438 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | B | protein | 376 | ORYCTOLAGUS CUNICULUS | P68135 (AlphaFold model) |
| Phosphatase and actin regulator 1 | M | protein | 32 | MUS MUSCULUS | Q2M3X8 (AlphaFold model) |
>4B1W_1 ACTIN, ALPHA SKELETAL MUSCLE (chains B) CDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVARPRHQGVMVGMGQKDSYVGDEAQ SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK QEYDEAGPSIVHRKCF
>4B1W_2 PHOSPHATASE AND ACTIN REGULATOR 1 (chains M) KVCRKDSLAIKLSNRPSKRELEEKNILPRQTD
| ID | Name | Formula | Copies |
|---|---|---|---|
| LAB | Latrunculin B | C20 H29 N O5 S | 1 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (SO4, GOL) are not listed.
Structures of the Phactr1 RPEL domain and RPEL motif complexes with G-actin reveal the molecular basis for actin binding cooperativity. Mouilleron, S., Wiezlak, M., O'Reilly, N. et al. Structure (2012) 20:1960-1970. DOI 10.1016/j.str.2012.08.031 · 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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