AP2 bound to heparin and Tgn38 tyrosine cargo peptide. Determined by electron microscopy at 4.7 Å resolution. Released 30 Mar 2022.
Explore 7RWA in 3D Show helices and sheets RCSB PDB PDBe
7RWA contains 174 α-helices and 80 β-strands across 10 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 | 12-21 | 10 | |
| α-helix | 26-44 | 19 | |
| α-helix | 53-68 | 16 | |
| α-helix | 77-83 | 7 | |
| α-helix | 88-100 | 13 | |
| α-helix | 107-120 | 14 | |
| α-helix | 125-137 | 13 | |
| α-helix | 141-145 | 5 | |
| α-helix | 150-155 | 6 | |
| α-helix | 162-178 | 17 | |
| α-helix | 189-192 | 4 | |
| α-helix | 195-197 | 3 | |
| α-helix | 201-217 | 17 | |
| α-helix | 219-222 | 4 | |
| α-helix | 225-237 | 13 | |
| α-helix | 245-247 | 3 | |
| β-strand | 248-249 | 2 | 11 |
| β-strand | 252-253 | 2 | 11 |
| α-helix | 255-265 | 11 | |
| α-helix | 269 | 1 | |
| α-helix | 271 | 1 | |
| 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 | 360-368 | 9 | |
| α-helix | 370-379 | 10 | |
| α-helix | 384-395 | 12 | |
| α-helix | 399-414 | 16 | |
| α-helix | 420-434 | 15 | |
| α-helix | 439-452 | 14 | |
| α-helix | 461-472 | 12 | |
| α-helix | 475-487 | 13 | |
| α-helix | 494-511 | 18 | |
| α-helix | 515-517 | 3 | |
| α-helix | 519-529 | 11 | |
| α-helix | 535-551 | 17 | |
| α-helix | 556-562 | 7 | |
| α-helix | 566-569 | 4 | |
| α-helix | 574-589 | 16 | |
| α-helix | 594-598 | 5 | |
| α-helix | 603-607 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 88-95 | 8 | |
| α-helix | 100-112 | 13 | |
| α-helix | 118-130 | 13 | |
| α-helix | 135-149 | 15 | |
| α-helix | 156-167 | 12 | |
| α-helix | 174-187 | 14 | |
| α-helix | 201-213 | 13 | |
| α-helix | 216-225 | 10 | |
| α-helix | 226-228 | 3 | |
| α-helix | 234-244 | 11 | |
| α-helix | 253-265 | 13 | |
| α-helix | 276-290 | 15 | |
| α-helix | 291-293 | 3 | |
| α-helix | 296-312 | 17 | |
| α-helix | 325-327 | 3 | |
| α-helix | 332-345 | 14 | |
| α-helix | 351-362 | 12 | |
| α-helix | 367-383 | 17 | |
| α-helix | 385-399 | 15 | |
| α-helix | 404-420 | 17 | |
| α-helix | 428-434 | 7 | |
| α-helix | 442-454 | 13 | |
| α-helix | 462-469 | 8 | |
| α-helix | 478-494 | 17 | |
| α-helix | 496-498 | 3 | |
| α-helix | 500-513 | 14 | |
| α-helix | 517-530 | 14 | |
| α-helix | 534-540 | 7 | |
| α-helix | 557-563 | 7 | |
| β-strand | 569 | 1 | 12 |
| α-helix | 570-574 | 5 | |
| α-helix | 578-580 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 13 |
| β-strand | 14-19 | 6 | 13 |
| α-helix | 26-32 | 7 | |
| α-helix | 33-37 | 5 | |
| β-strand | 47-49 | 3 | 13 |
| β-strand | 54-60 | 7 | 13 |
| β-strand | 63-69 | 7 | 13 |
| β-strand | 74 | 1 | 12 |
| α-helix | 75-93 | 19 | |
| α-helix | 98-102 | 5 | |
| α-helix | 105-115 | 11 | |
| β-strand | 116-117 | 2 | 14 |
| β-strand | 120-121 | 2 | 14 |
| β-strand | 171-185 | 15 | 15 |
| β-strand | 191-205 | 15 | 15 |
| β-strand | 211-216 | 6 | 16 |
| β-strand | 245-248 | 4 | 15 |
| β-strand | 253 | 1 | 16 |
| β-strand | 263-265 | 3 | 16 |
| α-helix | 267-268 | 2 | |
| β-strand | 270-272 | 3 | 15 |
| β-strand | 275-279 | 5 | 15 |
| α-helix | 283-285 | 3 | |
| β-strand | 287-290 | 4 | 17 |
| β-strand | 293-296 | 4 | 17 |
| β-strand | 300-309 | 10 | 17 |
| β-strand | 316 | 1 | 18 |
| β-strand | 318-325 | 8 | 15 |
| β-strand | 330-337 | 8 | 17 |
| β-strand | 341-345 | 5 | 15 |
| β-strand | 350-355 | 6 | 15 |
| β-strand | 359 | 1 | 18 |
| β-strand | 363-372 | 10 | 17 |
| α-helix | 373-374 | 2 | |
| α-helix | 383-385 | 3 | |
| β-strand | 386-392 | 7 | 15 |
| β-strand | 401-407 | 7 | 16 |
| α-helix | 415-417 | 3 | |
| β-strand | 418-433 | 16 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-9 | 8 | 19 |
| β-strand | 14-19 | 6 | 19 |
| α-helix | 25-40 | 16 | |
| β-strand | 50-52 | 3 | 19 |
| β-strand | 55-62 | 8 | 19 |
| β-strand | 65-71 | 7 | 19 |
| α-helix | 77-95 | 19 | |
| α-helix | 100-105 | 6 | |
| α-helix | 107-117 | 11 | |
| β-strand | 118-119 | 2 | 20 |
| β-strand | 122-123 | 2 | 20 |
| α-helix | 128-140 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 350-352 | 3 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| AP-2 complex subunit alpha-2 | A, a | protein | 630 | Mus musculus | P17427 (AlphaFold model) |
| AP-2 complex subunit beta | B, b | protein | 591 | Mus musculus | Q9DBG3 (AlphaFold model) |
| AP-2 complex subunit mu | M, m | protein | 435 | Mus musculus | P84091 (AlphaFold model) |
| AP-2 complex subunit sigma | S, s | protein | 142 | Mus musculus | P62743 (AlphaFold model) |
| Trans-Golgi network integral membrane protein TGN38 peptide | Y, y | protein | 15 | Mus musculus | Q62314 |
>7RWA_1 AP-2 complex subunit alpha-2 (chains A, a) MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVC KLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDL ASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSP DLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSA STDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSKKV QHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSE FSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSI REEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAA KTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRAL LLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLE EMPPFPERESSILAKLKKKKGGSGLEVLFQ
>7RWA_2 AP-2 complex subunit beta (chains B, b) MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQT DNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITE YLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANA VAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSI CERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQY VALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKE YATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRK YPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQV QLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEV VLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRK
>7RWA_3 AP-2 complex subunit mu (chains M, m) MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKR SNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGY PQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLES VNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQS IAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTK LEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAG MKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIK WVRYIGRSGIYETRC
>7RWA_4 AP-2 complex subunit sigma (chains S, s) MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYR RYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLA GEIRETSQTKVLKQLLMLQSLE
>7RWA_5 Trans-Golgi network integral membrane protein TGN38 peptide (chains Y, y) CKVTRRPKAADYQRL
Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Partlow, E.A., Cannon, K.S., Hollopeter, G. et al. Nat Struct Mol Biol (2022) 29:339-347. DOI 10.1038/s41594-022-00749-z · PubMed
Other PDB entries of the same protein (UniProt P17427 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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