Closed AP-2 clathrin adaptor complex in solution. Determined by electron microscopy at 2.55 Å resolution. Released 8 Apr 2026.
Explore 9PWA in 3D Show helices and sheets RCSB PDB PDBe
9PWA contains 101 α-helices and 35 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 | 11-22 | 12 | |
| α-helix | 26-45 | 20 | |
| α-helix | 49-51 | 3 | |
| α-helix | 52-68 | 17 | |
| α-helix | 76-83 | 8 | |
| α-helix | 88-100 | 13 | |
| α-helix | 106-121 | 16 | |
| α-helix | 125-138 | 14 | |
| α-helix | 141-147 | 7 | |
| α-helix | 150-156 | 7 | |
| α-helix | 162-178 | 17 | |
| α-helix | 180-182 | 3 | |
| α-helix | 189-194 | 6 | |
| α-helix | 195-197 | 3 | |
| α-helix | 201-217 | 17 | |
| α-helix | 220-222 | 3 | |
| α-helix | 225-238 | 14 | |
| β-strand | 248-249 | 2 | 1 |
| β-strand | 252-253 | 2 | 1 |
| α-helix | 255-264 | 10 | |
| α-helix | 265-267 | 3 | |
| α-helix | 274-292 | 19 | |
| α-helix | 294-295 | 2 | |
| α-helix | 300-320 | 21 | |
| α-helix | 324-338 | 15 | |
| α-helix | 343-356 | 14 | |
| α-helix | 363-368 | 6 | |
| α-helix | 370-378 | 9 | |
| α-helix | 383-396 | 14 | |
| α-helix | 402-415 | 14 | |
| α-helix | 418-435 | 18 | |
| α-helix | 439-453 | 15 | |
| α-helix | 459-471 | 13 | |
| α-helix | 476-487 | 12 | |
| α-helix | 494-507 | 14 | |
| α-helix | 508-510 | 3 | |
| α-helix | 515-517 | 3 | |
| α-helix | 519-530 | 12 | |
| α-helix | 535-551 | 17 | |
| α-helix | 553-555 | 3 | |
| α-helix | 556-563 | 8 | |
| α-helix | 566-569 | 4 | |
| α-helix | 574-588 | 15 | |
| α-helix | 592-598 | 7 | |
| α-helix | 603-605 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-22 | 9 | |
| α-helix | 27-43 | 17 | |
| α-helix | 48-50 | 3 | |
| α-helix | 51-56 | 6 | |
| α-helix | 63-79 | 17 | |
| α-helix | 81-84 | 4 | |
| α-helix | 85-87 | 3 | |
| α-helix | 88-92 | 5 | |
| α-helix | 100-112 | 13 | |
| α-helix | 118-130 | 13 | |
| α-helix | 135-150 | 16 | |
| α-helix | 156-167 | 12 | |
| α-helix | 174-187 | 14 | |
| α-helix | 200-213 | 14 | |
| α-helix | 216-226 | 11 | |
| α-helix | 234-244 | 11 | |
| α-helix | 254-265 | 12 | |
| α-helix | 277-283 | 7 | |
| α-helix | 285-290 | 6 | |
| α-helix | 291-293 | 3 | |
| α-helix | 296-312 | 17 | |
| α-helix | 322-324 | 3 | |
| α-helix | 325-327 | 3 | |
| α-helix | 332-344 | 13 | |
| α-helix | 351-362 | 12 | |
| α-helix | 367-383 | 17 | |
| α-helix | 388-400 | 13 | |
| α-helix | 404-420 | 17 | |
| α-helix | 426-428 | 3 | |
| α-helix | 429-434 | 6 | |
| α-helix | 442-453 | 12 | |
| α-helix | 456-458 | 3 | |
| α-helix | 462-470 | 9 | |
| α-helix | 478-494 | 17 | |
| α-helix | 500-508 | 9 | |
| α-helix | 509-513 | 5 | |
| α-helix | 517-530 | 14 | |
| α-helix | 536-541 | 6 | |
| α-helix | 543-548 | 6 | |
| 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 | 4-8 | 5 | 3 |
| β-strand | 14-19 | 6 | 3 |
| α-helix | 26-32 | 7 | |
| α-helix | 33-37 | 5 | |
| α-helix | 43-44 | 2 | |
| β-strand | 47-50 | 4 | 3 |
| β-strand | 53-60 | 8 | 3 |
| β-strand | 63-69 | 7 | 3 |
| β-strand | 74 | 1 | 2 |
| α-helix | 75-93 | 19 | |
| α-helix | 98-103 | 6 | |
| α-helix | 105-115 | 11 | |
| β-strand | 116-117 | 2 | 4 |
| β-strand | 120-121 | 2 | 4 |
| α-helix | 126-132 | 7 | |
| α-helix | 137-139 | 3 | |
| β-strand | 172-185 | 14 | 5 |
| β-strand | 191-205 | 15 | 5 |
| β-strand | 211-216 | 6 | 6 |
| β-strand | 245-248 | 4 | 5 |
| β-strand | 253-254 | 2 | 6 |
| β-strand | 263-265 | 3 | 6 |
| α-helix | 267-268 | 2 | |
| β-strand | 270-279 | 10 | 5 |
| β-strand | 287-294 | 8 | 7 |
| β-strand | 300-309 | 10 | 7 |
| β-strand | 316-325 | 10 | 5 |
| β-strand | 330-337 | 8 | 7 |
| β-strand | 341-345 | 5 | 5 |
| β-strand | 350-359 | 10 | 5 |
| β-strand | 362-372 | 11 | 7 |
| α-helix | 383-385 | 3 | |
| β-strand | 386-392 | 7 | 5 |
| β-strand | 401-407 | 7 | 6 |
| α-helix | 415-417 | 3 | |
| β-strand | 419-433 | 15 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 8 |
| β-strand | 14-19 | 6 | 8 |
| α-helix | 25-40 | 16 | |
| β-strand | 49-52 | 4 | 8 |
| β-strand | 55-62 | 8 | 8 |
| β-strand | 65-71 | 7 | 8 |
| α-helix | 77-94 | 18 | |
| α-helix | 100-105 | 6 | |
| α-helix | 107-117 | 11 | |
| β-strand | 118-119 | 2 | 9 |
| β-strand | 122-123 | 2 | 9 |
| α-helix | 128-140 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| AP-2 complex subunit alpha-2 | A | protein | 630 | Mus musculus | P17427 (AlphaFold model) |
| AP-2 complex subunit beta | B | protein | 591 | Mus musculus | Q9DBG3 (AlphaFold model) |
| AP-2 complex subunit mu | M | protein | 435 | Mus musculus | P84091 (AlphaFold model) |
| AP-2 complex subunit sigma | S | protein | 142 | Mus musculus | P62743 (AlphaFold model) |
>9PWA_1 AP-2 complex subunit alpha-2 (chains A) MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVC KLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDL ASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSP DLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSA STDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSKKV QHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSE FSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSI REEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAA KTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRAL LLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLE EMPPFPERESSILAKLKKKKGGSGLEVLFQ
>9PWA_2 AP-2 complex subunit beta (chains B) MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQT DNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITE YLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANA VAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSI CERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQY VALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKE YATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRK YPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQV QLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEV VLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRK
>9PWA_3 AP-2 complex subunit mu (chains M) MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKR SNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGY PQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLES VNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQS IAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTK LEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAG MKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIK WVRYIGRSGIYETRC
>9PWA_4 AP-2 complex subunit sigma (chains S) MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYR RYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLA GEIRETSQTKVLKQLLMLQSLE
Closed AP-2 clathrin adaptor complex in solution. 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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