Structure of AP-2 bound to the dileucine motif of CCDC32; combined map. Determined by electron microscopy at 2.64 Å resolution. Released 8 Apr 2026.
Explore 9PWB in 3D Show helices and sheets RCSB PDB PDBe
9PWB contains 94 α-helices and 18 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 |
|---|---|---|---|
| α-helix | 11-21 | 11 | |
| α-helix | 26-45 | 20 | |
| α-helix | 52-68 | 17 | |
| α-helix | 76-82 | 7 | |
| α-helix | 88-100 | 13 | |
| α-helix | 106-121 | 16 | |
| α-helix | 125-137 | 13 | |
| α-helix | 141-146 | 6 | |
| α-helix | 151-155 | 5 | |
| α-helix | 162-178 | 17 | |
| α-helix | 180-182 | 3 | |
| α-helix | 189-194 | 6 | |
| α-helix | 195-197 | 3 | |
| α-helix | 201-214 | 14 | |
| α-helix | 223-225 | 3 | |
| α-helix | 226-237 | 12 | |
| β-strand | 248 | 1 | 1 |
| β-strand | 253 | 1 | 1 |
| α-helix | 255-265 | 11 | |
| α-helix | 274-291 | 18 | |
| α-helix | 300-320 | 21 | |
| α-helix | 324-337 | 14 | |
| α-helix | 343-356 | 14 | |
| α-helix | 363-367 | 5 | |
| α-helix | 370-378 | 9 | |
| α-helix | 383-395 | 13 | |
| α-helix | 402-413 | 12 | |
| α-helix | 421-434 | 14 | |
| α-helix | 439-452 | 14 | |
| α-helix | 459-472 | 14 | |
| α-helix | 476-486 | 11 | |
| α-helix | 494-507 | 14 | |
| α-helix | 508-511 | 4 | |
| α-helix | 515-517 | 3 | |
| α-helix | 519-530 | 12 | |
| α-helix | 535-551 | 17 | |
| α-helix | 556-563 | 8 | |
| α-helix | 566-569 | 4 | |
| α-helix | 574-589 | 16 | |
| α-helix | 594-598 | 5 | |
| α-helix | 603-605 | 3 | |
| α-helix | 611-619 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-43 | 17 | |
| α-helix | 48-50 | 3 | |
| α-helix | 51-55 | 5 | |
| α-helix | 56-58 | 3 | |
| α-helix | 63-73 | 11 | |
| α-helix | 82-84 | 3 | |
| α-helix | 85-94 | 10 | |
| α-helix | 100-111 | 12 | |
| α-helix | 116-119 | 4 | |
| α-helix | 123-129 | 7 | |
| α-helix | 135-149 | 15 | |
| α-helix | 156-161 | 6 | |
| α-helix | 164-169 | 6 | |
| α-helix | 174-188 | 15 | |
| α-helix | 201-210 | 10 | |
| α-helix | 216-226 | 11 | |
| α-helix | 234-244 | 11 | |
| α-helix | 245-248 | 4 | |
| α-helix | 253-265 | 13 | |
| α-helix | 275-283 | 9 | |
| α-helix | 285-290 | 6 | |
| α-helix | 291-293 | 3 | |
| α-helix | 296-312 | 17 | |
| α-helix | 322-324 | 3 | |
| α-helix | 326-327 | 2 | |
| α-helix | 332-345 | 14 | |
| α-helix | 351-361 | 11 | |
| α-helix | 367-383 | 17 | |
| α-helix | 385-387 | 3 | |
| α-helix | 388-399 | 12 | |
| α-helix | 404-420 | 17 | |
| α-helix | 429-432 | 4 | |
| α-helix | 442-454 | 13 | |
| α-helix | 462-467 | 6 | |
| α-helix | 470-475 | 6 | |
| α-helix | 478-494 | 17 | |
| α-helix | 500-511 | 12 | |
| α-helix | 517-532 | 16 | |
| α-helix | 534-541 | 8 | |
| α-helix | 554-556 | 3 | |
| α-helix | 557-564 | 8 | |
| β-strand | 569 | 1 | 2 |
| α-helix | 571-574 | 4 | |
| α-helix | 578-580 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 3 |
| β-strand | 16-18 | 3 | 3 |
| α-helix | 28-32 | 5 | |
| α-helix | 33-37 | 5 | |
| β-strand | 47-49 | 3 | 3 |
| β-strand | 54-60 | 7 | 3 |
| β-strand | 63-69 | 7 | 3 |
| β-strand | 74 | 1 | 2 |
| α-helix | 75-93 | 19 | |
| α-helix | 98-103 | 6 | |
| α-helix | 106-114 | 9 | |
| β-strand | 116-117 | 2 | 4 |
| β-strand | 120-121 | 2 | 4 |
| α-helix | 129-132 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-9 | 8 | 5 |
| β-strand | 14-19 | 6 | 5 |
| α-helix | 25-41 | 17 | |
| β-strand | 49-52 | 4 | 5 |
| β-strand | 55-62 | 8 | 5 |
| β-strand | 65-71 | 7 | 5 |
| α-helix | 77-94 | 18 | |
| α-helix | 100-105 | 6 | |
| α-helix | 107-117 | 11 | |
| β-strand | 118-119 | 2 | 6 |
| β-strand | 122-123 | 2 | 6 |
| α-helix | 128-140 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| AP-2 complex subunit alpha-2 | A | protein | 613 | Mus musculus | P17427 (AlphaFold model) |
| AP-2 complex subunit beta | B | protein | 557 | Mus musculus | Q9DBG3 (AlphaFold model) |
| Coiled-coil domain-containing protein 32 | C | protein | 11 | Mus musculus | Q8BS39 (AlphaFold model) |
| AP-2 complex subunit mu | M | protein | 135 | Mus musculus | P84091 (AlphaFold model) |
| AP-2 complex subunit sigma | S | protein | 141 | Mus musculus | P62744 |
>9PWB_1 AP-2 complex subunit alpha-2 (chains A) GMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLL GHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFM GLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDW TSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYT YYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNA VLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKT HIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSIREEIVLKV AILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAAKTVFEALQ APACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRALLLSTYIKF VNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLEEMPPFPER ESSILAKLKKKKG
>9PWB_2 AP-2 complex subunit beta (chains B) KKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAI MAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCV AKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANAVAALSEISESHPNSNLLDLNPQNIN KLLTALNECTEWGQIFILDCLSNYNPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMK FLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQYVALRNINLIVQKRPEILKQEIKVFF VKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVE QSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRKYPNKYESIIATLCENLDSLDEPDAR AAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLTLLTAIVKLFLKKPSETQELVQQ VLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEVVLSEKPLISEETDLIEPTLLDELIC HIGSLASVYHKPPNAFV
>9PWB_3 Coiled-coil domain-containing protein 32 (chains C) STEEVQFLIPP
>9PWB_4 AP-2 complex subunit mu (chains M) MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKR SNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGY PQNSETGALKTFITQ
>9PWB_5 AP-2 complex subunit sigma (chains S) MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYR RYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLA GEIRETSQTKVLKQLLMLQSL
Structure of AP-2 bound to the dileucine motif of CCDC32; combined map. Baker, R.W., Kikkawa, M., Sloan, D.E. et al. To be published.
Other PDB entries of the same protein (UniProt P17427 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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