9XYE: Two CAP-1
Two CAP-1 Bound to the Pointed End of F-actin. Determined by electron microscopy at 3.18 Å resolution. Released 4 Mar 2026.
- Method
- Electron microscopy
- Resolution
- 3.18 Å
- Organisms
- Oryctolagus cuniculus, Homo sapiens
- Chains
- 7
- Atoms
- 17,356
- Mol. weight
- 316.09 kDa
- Ligands
- ADP, MG
- Released
- 4 Mar 2026
Explore 9XYE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9XYE contains 132 α-helices and 96 β-strands across 7 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.
Chain A: 21 helices, 18 β-strands
| 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 | 56-60 | 5 | |
| 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 | 137-143 | 7 | |
| β-strand | 149-155 | 7 | 4 |
| β-strand | 160-166 | 7 | 4 |
| β-strand | 169-170 | 2 | 4 |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 182-196 | 15 | |
| α-helix | 206-215 | 10 | |
| α-helix | 223-231 | 9 | |
| β-strand | 240-241 | 2 | 5 |
| β-strand | 247-248 | 2 | 5 |
| α-helix | 252-254 | 3 | |
| α-helix | 259-261 | 3 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-284 | 11 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 303-305 | 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 | 366-368 | 3 | |
| α-helix | 370-373 | 4 | |
Chain B: 19 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 6 |
| β-strand | 16-21 | 6 | 6 |
| β-strand | 29-32 | 4 | 6 |
| β-strand | 35-37 | 3 | 7 |
| α-helix | 56-60 | 5 | |
| 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 | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 6 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 6 |
| α-helix | 137-143 | 7 | |
| β-strand | 149-155 | 7 | 9 |
| β-strand | 160-166 | 7 | 9 |
| β-strand | 169-170 | 2 | 9 |
| β-strand | 176-178 | 3 | 9 |
| α-helix | 182-194 | 13 | |
| α-helix | 206-215 | 10 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 10 |
| β-strand | 247-250 | 4 | 10 |
| α-helix | 252-254 | 3 | |
| α-helix | 258-261 | 4 | |
| α-helix | 274-284 | 11 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 9 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 9 |
| α-helix | 338-347 | 10 | |
| β-strand | 357-358 | 2 | 6 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-368 | 3 | |
| α-helix | 370-373 | 4 | |
Chain C: 24 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 11 |
| β-strand | 16-21 | 6 | 11 |
| β-strand | 29-32 | 4 | 11 |
| β-strand | 35-38 | 4 | 12 |
| β-strand | 41-42 | 2 | 4 |
| β-strand | 53-54 | 2 | 12 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 12 |
| β-strand | 71-72 | 2 | 13 |
| β-strand | 75-76 | 2 | 13 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 11 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 11 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 14 |
| β-strand | 160-166 | 7 | 14 |
| β-strand | 169-170 | 2 | 14 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 14 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 15 |
| β-strand | 247-250 | 4 | 15 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 14 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 14 |
| α-helix | 338-347 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 11 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-368 | 3 | |
| α-helix | 370-373 | 4 | |
Chain D: 25 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 16 |
| β-strand | 16-21 | 6 | 16 |
| β-strand | 29-32 | 4 | 16 |
| β-strand | 35-38 | 4 | 17 |
| β-strand | 41-42 | 2 | 9 |
| β-strand | 53-54 | 2 | 17 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 17 |
| β-strand | 71-72 | 2 | 18 |
| β-strand | 75-76 | 2 | 18 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 16 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 16 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 19 |
| β-strand | 160-166 | 7 | 19 |
| β-strand | 169-170 | 2 | 19 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 19 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 20 |
| β-strand | 247-250 | 4 | 20 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-266 | 3 | |
| 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 | 19 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 19 |
| α-helix | 338-347 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 16 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-368 | 3 | |
| α-helix | 370-373 | 4 | |
Chain E: 25 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 21 |
| β-strand | 16-21 | 6 | 21 |
| β-strand | 29-32 | 4 | 21 |
| β-strand | 35-38 | 4 | 22 |
| β-strand | 41-42 | 2 | 14 |
| β-strand | 53-54 | 2 | 22 |
| α-helix | 56-60 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 22 |
| β-strand | 71-72 | 2 | 23 |
| β-strand | 75-76 | 2 | 23 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 21 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 21 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-155 | 6 | 24 |
| β-strand | 160-166 | 7 | 24 |
| β-strand | 169-170 | 2 | 24 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 24 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 25 |
| β-strand | 247-250 | 4 | 25 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| 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 | 24 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 24 |
| α-helix | 338-347 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 21 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-368 | 3 | |
| α-helix | 370-373 | 4 | |
Chain W: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 42-50 | 9 | |
| α-helix | 51-55 | 5 | |
| α-helix | 56-65 | 10 | |
| α-helix | 68-91 | 24 | |
| α-helix | 98-121 | 24 | |
| α-helix | 128-135 | 8 | |
| α-helix | 138-145 | 8 | |
| α-helix | 151-172 | 22 | |
| α-helix | 177-199 | 23 | |
Chain X: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 42-50 | 9 | |
| α-helix | 51-55 | 5 | |
| α-helix | 56-65 | 10 | |
| α-helix | 68-92 | 25 | |
| α-helix | 98-121 | 24 | |
| α-helix | 128-135 | 8 | |
| α-helix | 138-145 | 8 | |
| α-helix | 151-171 | 21 | |
| α-helix | 177-200 | 24 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Actin, alpha skeletal muscle | A, B, C, D, E | protein | 376 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Adenylyl cyclase-associated protein 1 | W, X | protein | 475 | Homo sapiens | Q01518 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>9XYE_1 Actin, alpha skeletal muscle (chains A, B, C, D, E)
CDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK
QEYDEAGPSIVHRKCF
Sequence of entity 2 (W, X), FASTA
>9XYE_2 Adenylyl cyclase-associated protein 1 (chains W, X)
MADMQNLVERLERAVGRLEAVSHTSDMHRGYADSPSKAGAAPYVQAFDSLLAGPVAEYLK
ISKEIGGDVQKHAEMVHTGLKLERALLVTASQCQQPAENKLSDLLAPISEQIKEVITFRE
KNRGSKLFNHLSAVSESIQALGWVAMAPKPGPYVKEMNDAAMFYTNRVLKEYKDVDKKHV
DWVKAYLSIWTELQAYIKEFHTTGLAWSKTGPVAKELSGLPSGPSAGSCPPPPPPCPPPP
PVSTISCSYESASRSSLFAQINQGESITHALKHVSDDMKTHKNPALKAQSGPVRSGPKPF
SAPKPQTSPSPKRATKKEPAVLELEGKKWRVENQENVSNLVIEDTELKQVAYIYKCVNTT
LQIKGKINSITVDNCKKLGLVFDDVVGIVEIINSKDVKVQVMGKVPTISINKTDGCHAYL
SKNSLDCEIVSAKSSEMNVLIPTEGGDFNEFPVPEQFKTLWNGQKLVTTVTEIAG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 5 |
| MG | Magnesium ion | Mg | 5 |
Primary citation
Mechanisms of disassembly at the actin filament pointed and barbed ends. Palmer, N.J., Boczkowska, M., Rebowski, G. et al. Sci Adv (2026) 12:eaee5882-eaee5882. DOI 10.1126/sciadv.aee5882 · PubMed
Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4B1Y 1.29 Å, Structure of the Phactr1 RPEL-3 bound to G-actin
- 2FXU 1.35 Å, X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
- 4K41 1.4 Å, Crystal structure of actin in complex with marine macrolide kabiramide C
- 1QZ5 1.45 Å, Structure of rabbit actin in complex with kabiramide C
- 1WUA 1.45 Å, The structure of Aplyronine A-actin complex
- 2Q0U 1.45 Å, Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin
- 2V52 1.45 Å, Structure of MAL-RPEL2 complexed to G-actin
- 3MN5 1.5 Å, Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation
- 2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
- 5ZZA 1.53 Å, OdinProfilin/Rabbit Actin Complex
- 1J6Z 1.54 Å, Uncomplexed actin
- 1QZ6 1.6 Å, Structure of rabbit actin in complex with jaspisamide A
Browse structure collections
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