9RTX: Mammalian AP3 complex on tubular membranes
Mammalian AP3 complex on tubular membranes (ARF1 centered Beta3-ARF1 dimer-Beta3 interface). Determined by electron microscopy at 8.5 Å resolution. Released 27 May 2026.
- Method
- Electron microscopy
- Resolution
- 8.5 Å
- Organisms
- Pan troglodytes, Homo sapiens, Rattus norvegicus
- Chains
- 14
- Atoms
- 18,000
- Mol. weight
- 682.35 kDa
- Released
- 27 May 2026
Explore 9RTX in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9RTX contains 281 α-helices and 126 β-strands across 14 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 b: 46 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 44-52 | 9 | |
| α-helix | 56-71 | 16 | |
| α-helix | 77-79 | 3 | |
| α-helix | 80-84 | 5 | |
| α-helix | 85-88 | 4 | |
| α-helix | 92-105 | 14 | |
| α-helix | 110-123 | 14 | |
| α-helix | 129-141 | 13 | |
| α-helix | 145-147 | 3 | |
| α-helix | 148-159 | 12 | |
| α-helix | 164-180 | 17 | |
| α-helix | 182-184 | 3 | |
| α-helix | 185-196 | 12 | |
| α-helix | 201-214 | 14 | |
| α-helix | 220-223 | 4 | |
| α-helix | 226-232 | 7 | |
| α-helix | 233-235 | 3 | |
| α-helix | 238-255 | 18 | |
| α-helix | 295-304 | 10 | |
| α-helix | 305-309 | 5 | |
| β-strand | 310 | 1 | 1 |
| α-helix | 313-326 | 14 | |
| α-helix | 329-332 | 4 | |
| α-helix | 335-342 | 8 | |
| α-helix | 347-363 | 17 | |
| α-helix | 365-367 | 3 | |
| α-helix | 369-375 | 7 | |
| α-helix | 376-378 | 3 | |
| α-helix | 383-396 | 14 | |
| α-helix | 402-412 | 11 | |
| α-helix | 418-434 | 17 | |
| α-helix | 436-438 | 3 | |
| α-helix | 439-449 | 11 | |
| α-helix | 455-470 | 16 | |
| α-helix | 477-486 | 10 | |
| α-helix | 493-505 | 13 | |
| α-helix | 513-524 | 12 | |
| α-helix | 525-527 | 3 | |
| α-helix | 530-546 | 17 | |
| α-helix | 548-563 | 16 | |
| α-helix | 568-581 | 14 | |
| α-helix | 589-592 | 4 | |
| α-helix | 594-599 | 6 | |
| α-helix | 603-606 | 4 | |
| α-helix | 612-614 | 3 | |
| α-helix | 618 | 1 | |
| α-helix | 622-626 | 5 | |
Chain B: 47 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 44-52 | 9 | |
| α-helix | 56-71 | 16 | |
| α-helix | 77-79 | 3 | |
| α-helix | 80-84 | 5 | |
| α-helix | 85-88 | 4 | |
| α-helix | 92-105 | 14 | |
| α-helix | 110-123 | 14 | |
| α-helix | 129-141 | 13 | |
| α-helix | 145-147 | 3 | |
| α-helix | 148-159 | 12 | |
| α-helix | 164-180 | 17 | |
| α-helix | 182-184 | 3 | |
| α-helix | 185-196 | 12 | |
| α-helix | 201-214 | 14 | |
| α-helix | 219-221 | 3 | |
| α-helix | 223-225 | 3 | |
| α-helix | 226-232 | 7 | |
| α-helix | 233-235 | 3 | |
| α-helix | 238-255 | 18 | |
| α-helix | 295-304 | 10 | |
| α-helix | 305-309 | 5 | |
| β-strand | 310 | 1 | 15 |
| α-helix | 313-326 | 14 | |
| α-helix | 329-332 | 4 | |
| α-helix | 335-342 | 8 | |
| α-helix | 347-363 | 17 | |
| α-helix | 365-367 | 3 | |
| α-helix | 369-375 | 7 | |
| α-helix | 376-378 | 3 | |
| α-helix | 383-396 | 14 | |
| α-helix | 402-412 | 11 | |
| α-helix | 418-434 | 17 | |
| α-helix | 436-438 | 3 | |
| α-helix | 439-449 | 11 | |
| α-helix | 455-470 | 16 | |
| α-helix | 477-486 | 10 | |
| α-helix | 493-505 | 13 | |
| α-helix | 513-524 | 12 | |
| α-helix | 525-527 | 3 | |
| α-helix | 530-546 | 17 | |
| α-helix | 548-563 | 16 | |
| α-helix | 568-581 | 14 | |
| α-helix | 589-592 | 4 | |
| α-helix | 594-599 | 6 | |
| α-helix | 603-606 | 4 | |
| α-helix | 612-614 | 3 | |
| α-helix | 618 | 1 | |
| α-helix | 622-626 | 5 | |
Chains d and D: 45 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-27 | 9 | |
| α-helix | 32-47 | 16 | |
| α-helix | 52-67 | 16 | |
| α-helix | 73-75 | 3 | |
| α-helix | 76-83 | 8 | |
| α-helix | 88-101 | 14 | |
| α-helix | 107-111 | 5 | |
| α-helix | 112-120 | 9 | |
| α-helix | 125-138 | 14 | |
| α-helix | 141-154 | 14 | |
| α-helix | 160-176 | 17 | |
| α-helix | 178-180 | 3 | |
| α-helix | 181-190 | 10 | |
| α-helix | 191-193 | 3 | |
| α-helix | 197-213 | 17 | |
| α-helix | 215-221 | 7 | |
| α-helix | 222-231 | 10 | |
| α-helix | 235-248 | 14 | |
| α-helix | 249-251 | 3 | |
| α-helix | 253-269 | 17 | |
| α-helix | 273-289 | 17 | |
| α-helix | 297-313 | 17 | |
| α-helix | 317-331 | 15 | |
| α-helix | 335-339 | 5 | |
| α-helix | 342-348 | 7 | |
| α-helix | 354-367 | 14 | |
| α-helix | 373-385 | 13 | |
| α-helix | 389-409 | 21 | |
| α-helix | 415-425 | 11 | |
| α-helix | 434-447 | 14 | |
| α-helix | 449-451 | 3 | |
| α-helix | 452-464 | 13 | |
| α-helix | 466-469 | 4 | |
| α-helix | 480-491 | 12 | |
| α-helix | 493-495 | 3 | |
| α-helix | 499-506 | 8 | |
| α-helix | 509-513 | 5 | |
| α-helix | 516-539 | 24 | |
| α-helix | 543-556 | 14 | |
| α-helix | 558-561 | 4 | |
| α-helix | 566-586 | 21 | |
| α-helix | 593-598 | 6 | |
| α-helix | 612-614 | 3 | |
| α-helix | 615-618 | 4 | |
| α-helix | 629-631 | 3 | |
Chains E, F, G, H, I and J: 8 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 16-24 | 9 | 16 |
| α-helix | 30-38 | 9 | |
| β-strand | 43 | 1 | 17 |
| β-strand | 51-58 | 8 | 16 |
| β-strand | 61-68 | 8 | 16 |
| α-helix | 75-81 | 7 | |
| β-strand | 87-93 | 7 | 16 |
| α-helix | 97-99 | 3 | |
| α-helix | 100-111 | 12 | |
| α-helix | 114-116 | 3 | |
| β-strand | 120-126 | 7 | 16 |
| α-helix | 136-143 | 8 | |
| α-helix | 145-147 | 3 | |
| β-strand | 153-157 | 5 | 16 |
| β-strand | 159 | 1 | 18 |
| β-strand | 164 | 1 | 18 |
| α-helix | 166-177 | 12 | |
Chains m and M: 17 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 7 |
| β-strand | 14-19 | 6 | 7 |
| α-helix | 26-29 | 4 | |
| α-helix | 30-38 | 9 | |
| α-helix | 42-44 | 3 | |
| β-strand | 48-50 | 3 | 7 |
| β-strand | 55-61 | 7 | 7 |
| β-strand | 64-70 | 7 | 7 |
| α-helix | 76-94 | 19 | |
| α-helix | 99-104 | 6 | |
| α-helix | 106-116 | 11 | |
| β-strand | 117-118 | 2 | 8 |
| β-strand | 121-122 | 2 | 8 |
| α-helix | 127-133 | 7 | |
| β-strand | 134 | 1 | 9 |
| α-helix | 135-137 | 3 | |
| α-helix | 139-148 | 10 | |
| β-strand | 153 | 1 | 9 |
| α-helix | 159-162 | 4 | |
| β-strand | 178-191 | 14 | 1 |
| β-strand | 197-211 | 15 | 1 |
| β-strand | 217-222 | 6 | 10 |
| α-helix | 225-227 | 3 | |
| β-strand | 228-233 | 6 | 1 |
| β-strand | 237 | 1 | 10 |
| α-helix | 239-245 | 7 | |
| β-strand | 248-250 | 3 | 10 |
| α-helix | 252-253 | 2 | |
| β-strand | 255-264 | 10 | 1 |
| α-helix | 269-271 | 3 | |
| β-strand | 274-282 | 9 | 11 |
| β-strand | 288-297 | 10 | 11 |
| α-helix | 303-304 | 2 | |
| β-strand | 305-313 | 9 | 1 |
| β-strand | 318-325 | 8 | 11 |
| β-strand | 329-333 | 5 | 1 |
| β-strand | 338-344 | 7 | 1 |
| β-strand | 347 | 1 | 12 |
| β-strand | 350 | 1 | 12 |
| β-strand | 353-360 | 8 | 11 |
| α-helix | 364-367 | 4 | |
| α-helix | 370-372 | 3 | |
| β-strand | 373-380 | 8 | 1 |
| β-strand | 389-395 | 7 | 10 |
| β-strand | 402-416 | 15 | 1 |
Chains s and S: 8 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 13 |
| β-strand | 14-19 | 6 | 13 |
| α-helix | 25-40 | 16 | |
| β-strand | 49-51 | 3 | 13 |
| α-helix | 52-53 | 2 | |
| α-helix | 54-56 | 3 | |
| α-helix | 58-60 | 3 | |
| β-strand | 61-68 | 8 | 13 |
| β-strand | 71-78 | 8 | 13 |
| α-helix | 83-101 | 19 | |
| α-helix | 106-111 | 6 | |
| α-helix | 113-123 | 11 | |
| β-strand | 124-125 | 2 | 14 |
| β-strand | 128-129 | 2 | 14 |
| α-helix | 134-152 | 19 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| AP-3 complex subunit beta | B, b | protein | 658 | Pan troglodytes | A0A2I3SW12 (AlphaFold model) |
| AP-3 complex subunit delta | D, d | protein | 1203 | Homo sapiens | A0A8V8TQW4 (AlphaFold model) |
| ADP-ribosylation factor 1 | E, F, G, H, I, J | protein | 181 | Homo sapiens | P84077 (AlphaFold model) |
| AP-3 complex subunit mu-1 | M, m | protein | 418 | Rattus norvegicus | A6KKR5 (AlphaFold model) |
| AP-3 complex subunit sigma-1 | S, s | protein | 193 | Homo sapiens | Q92572 |
Sequence of entity 1 (B, b), FASTA
>9RTX_1 AP-3 complex subunit beta (chains B, b)
HHHHHHHHHHMASNSFPYNEQSGGGEATELGQEATSTISPSGAFGLFSSDLKKNEDLKQM
LESNKDSAKLDAMKRIVGMIAKGKNASELFPAVVKNVASKNIEIKKLVYVYLVRYAEEQQ
DLALLSISTFQRALKDPNQLIRASALRVLSSIRVPIIVPIMMLAIKEASADLSPYVRKNA
AHAIQKLYSLDPEQKEMLIEVIEKLLKDKSTLVAGSVVMAFEEVCPDRIDLIHKNYRKLC
NLLVDVEEWGQVVIIHMLTRYARTQFVSPWKEGDELEDNGKNFYESDDDQKEKTDKKKKP
YTMDPDHRLLIRNTKPLLQSRNAAVVMAVAQLYWHISPKSEAGIISKSLVRLLRSNREVQ
YIVLQNIATMSIQRKGMFEPYLKSFYVRSTDPTMIKTLKLEILTNLANEANISTLLREFQ
TYVKSQDKQFAAATIQTIGRCATNILEVTDTCLNGLVCLLSNRDEIVVAESVVVIKKLLQ
MQPAQHGEIIKHMAKLLDSITVPVARASILWLIGENCERVPKIAPDVLRKMAKSFTSEDD
LVKLQILNLGAKLYLTNSKQTKLLTQYILNLGKYDQNYDIRDRTRFIRQLIVPNEKSGAL
SKYAKKIFLAQKPAPLLESPFKDRDHFQLGTLSHTLNIKATGYLELSNWPEVAPDPSV
Sequence of entity 2 (D, d), FASTA
>9RTX_2 AP-3 complex subunit delta (chains D, d)
MALKMVKGSIDRMFDKNLQDLVRGIRNHKEDEAKYISQCIDEIKQELKQDNIAVKANAVC
KLTYLQMLGYDISWAAFNIIEVMSASKFTFKRIGYLAASQSFHEGTNVIMLTTNQIRKDL
SSPSQYDTGVALTGLSCFVTPDLARDLANDIMTLMSHTKPYIRKKAVLIMYKVFLKYPES
LRPAFPRLKEKLEDPDPGVQSAAVNVICELARRNPKNYLSLAPLFFKLMTSSTNNWVLIK
IIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECVNTVIAVLISLSSGMPNHSAS
IQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQSHKDLILQCLDDKDESIRLRA
LDLLYGMVSKKNLMEIVKKLMTHVDKAEGTTYRDELLTKIIDICSQSNYQYITNFEWYIS
ILVELTRLEGTRHGHLIAAQMLDVAIRVKAIRKFAVSQMSALLDSAHLLASSTQRNGICE
VLYAAAWICGEFSEHLQEPHHTLEAMLRPRVTTLPGHIQAVYVQNVVKLYASILQQKEQA
GEAEGAQAVTQLMVDRLPQFVQSADLEVQERASCILQLVKHIQKLQAKDVPVAEEVSALF
AGELNPVAPKAQKKVPVPEGLDLDAWINEPLSDSESEDERPRAVFHEEEQRRPKHRPSEA
DEEELARRREARKQEQANNPFYIKSSPSPQKRYQDTPGVEHIPVVQIDLSVPLKVPGLPM
SDQYVKLEEERRHRQKLEKDKRRKKRKEKEKKGKRRHSSLPTESDEDIAPAQQVDIVTEE
MPENALPSDEDDKDPNDPYRALDIDLDKPLADSEKLPIQKHRNTETSKSPEKDVPMVEKK
SKKPKKKEKKHKEKERDKEKKKEKEKKAEDLDFWLSTTPPPAPAPAPAPVPSTDECEDAK
TEAQGEEDDAEGQDQDKKSPKPKKKKHRKEKEERTKGKKKSKKQPPGSEEAAGEPVQNGA
PEEEQLPPESSYSLLAENSYVKMTCDIRGSLQEDSQVTVAIVLENRSSSILKGMELSVLD
SLNARMARPQGSSVHDGVPVPFQLPPGVSNEAQYVFTIQSIVMAQKLKGTLSFIAKNDEG
ATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMSSIKVDGIRMSFQNLLAKICF
HHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGENSVSVDGKCSDSTLLSNLLEEMKATL
AKC
Sequence of entity 3 (E, F, G, H, I, J), FASTA
>9RTX_3 ADP-ribosylation factor 1 (chains E, F, G, H, I, J)
MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKN
ISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAV
LLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQ
K
Sequence of entity 4 (M, m), FASTA
>9RTX_4 AP-3 complex subunit mu-1 (chains M, m)
MIHSLFLINCSGDIFLEKHWKSVVSQSVCDYFFEAQEKAADVENVPPVISTPHHYLISIY
RDKLFFVSVIQTEVSPLFVIEFLHRVADTFQDYFGECSEAAIKDNVVIVYELLEEMLDNG
FPLATESNILKELIKPPTILRSVVNSITGSSNVGDTLPTGQLSNIPWRRAGVKYTNNEAY
FDVVEEIDAIIDKSGSTVFAEIQGVIDACIKLSGMPDLSLSFMNPRLLDDVSFHPCIRFK
RWESERVLSFIPPDGNFRLISYRVSSQNLVAIPVYVKHNISFKENSSCGRFDITIGPKQN
MGKTIEGITVTVHMPKVVLNMNLTPTQGSYTFDPVTKVLAWDVGKITPQKLPSLKGLVNL
QSGAPKPEENPNLNIQFKIQQLAISGLKVNRLDMYGEKYKPFKGVKYITKAGKFQVRT
Sequence of entity 5 (S, s), FASTA
>9RTX_5 AP-3 complex subunit sigma-1 (chains S, s)
MIKAILIFNNYGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEGGLLIGGSD
NKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHNIL
AEMVMGGMVLETNMNEIVTQIDAQNKLEKSEAGLAGAPARAVSAVKNMNLPEIPRNINIG
DISIKVPNLPSFK
Primary citation
Architecture of clathrin-independent AP3:ARF1-coated carriers. Kaufman, J.G.G., Tagiltsev, G., Stalder, D.S. et al. Sci Adv (2026) 12:eaed1529-eaed1529. DOI 10.1126/sciadv.aed1529 · PubMed
Other PDB entries of the same protein (UniProt A0A2I3SW12 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9RTW 7.4 Å, Mammalian AP3 complex on tubular membranes (AP3 centered)
- 9RTY 8.9 Å, Mammalian AP3 complex on tubular membranes (ARF1 centered Beta3-ARF1 dimer-Delta…
- 9RTZ 13.0 Å, Mammalian AP3 complex on tubular membranes (ARF1 centered Delta-ARF1 dimer-Delta3…
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