Structure of the Phactr1 RPEL-N domain bound to G-actin. Determined by X-ray diffraction at 1.75 Å resolution. Released 7 Nov 2012.
Explore 4B1V in 3D Show helices and sheets RCSB PDB PDBe
4B1V contains 54 α-helices and 38 β-strands across 4 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 | 35-36 | 2 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-59 | 4 | |
| β-strand | 67-68 | 2 | 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 | 182-193 | 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 | 274-283 | 10 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| α-helix | 325-327 | 3 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 335-337 | 3 | |
| 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 | 6-7 | 2 | |
| β-strand | 8-12 | 5 | 6 |
| β-strand | 16-21 | 6 | 6 |
| β-strand | 29-32 | 4 | 6 |
| β-strand | 35-37 | 3 | 7 |
| β-strand | 53-54 | 2 | 7 |
| α-helix | 56-59 | 4 | |
| β-strand | 66-68 | 3 | 7 |
| β-strand | 71-72 | 2 | 8 |
| β-strand | 75-76 | 2 | 8 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 6 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 6 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 9 |
| β-strand | 160-166 | 7 | 9 |
| β-strand | 169-170 | 2 | 9 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 9 |
| 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 | 10 |
| β-strand | 247-250 | 4 | 10 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 9 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| α-helix | 325-327 | 3 | |
| β-strand | 329-330 | 2 | 9 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 6 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 138-145 | 8 | |
| α-helix | 147-149 | 3 | |
| α-helix | 150-155 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A, B | protein | 376 | ORYCTOLAGUS CUNICULUS | P68135 (AlphaFold model) |
| Phosphatase and actin regulator 1 | M, N | protein | 32 | MUS MUSCULUS | Q2M3X8 (AlphaFold model) |
>4B1V_1 ACTIN, ALPHA SKELETAL MUSCLE (chains A, B) CDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK QEYDEAGPSIVHRKCF
>4B1V_2 PHOSPHATASE AND ACTIN REGULATOR 1 (chains M, N) FKHTSAALERKISMRQSREELIKRGVLKEIYD
| ID | Name | Formula | Copies |
|---|---|---|---|
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 2 |
| LAB | Latrunculin B | C20 H29 N O5 S | 2 |
| MG | Magnesium ion | Mg | 2 |
Water and common crystallization additives (EDO, 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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