Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of INO80. Determined by electron microscopy at 3.3 Å resolution. Released 14 Dec 2022.
Explore 8A5A in 3D Show helices and sheets RCSB PDB PDBe
8A5A contains 95 α-helices and 72 β-strands across 5 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 | 459-478 | 20 | |
| α-helix | 479-485 | 7 | |
| α-helix | 486-513 | 28 | |
| α-helix | 514-518 | 5 | |
| α-helix | 522-559 | 38 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 167-177 | 11 | |
| α-helix | 197-199 | 3 | |
| β-strand | 206 | 1 | 1 |
| α-helix | 216-227 | 12 | |
| β-strand | 268-272 | 5 | 2 |
| β-strand | 277-281 | 5 | 2 |
| β-strand | 289-292 | 4 | 2 |
| β-strand | 295-298 | 4 | 3 |
| α-helix | 299-301 | 3 | |
| α-helix | 309-310 | 2 | |
| α-helix | 321-340 | 20 | |
| α-helix | 349-359 | 11 | |
| α-helix | 362 | 1 | |
| β-strand | 363-365 | 3 | 4 |
| α-helix | 367-369 | 3 | |
| β-strand | 377 | 1 | 5 |
| β-strand | 384-385 | 2 | 3 |
| α-helix | 386-391 | 6 | |
| β-strand | 392 | 1 | 5 |
| β-strand | 397-400 | 4 | 3 |
| β-strand | 403-404 | 2 | 6 |
| β-strand | 407-408 | 2 | 6 |
| α-helix | 418-433 | 16 | |
| α-helix | 445-447 | 3 | |
| β-strand | 449-454 | 6 | 2 |
| α-helix | 460-468 | 9 | |
| α-helix | 469-473 | 5 | |
| β-strand | 478-483 | 6 | 2 |
| α-helix | 484-492 | 9 | |
| β-strand | 498-503 | 6 | 7 |
| β-strand | 508-514 | 7 | 7 |
| β-strand | 517-518 | 2 | 7 |
| α-helix | 520-522 | 3 | |
| β-strand | 524-526 | 3 | 7 |
| α-helix | 530-543 | 14 | |
| α-helix | 556-569 | 14 | |
| α-helix | 574-576 | 3 | |
| β-strand | 580-585 | 6 | 4 |
| β-strand | 593-600 | 8 | 4 |
| α-helix | 603-609 | 7 | |
| α-helix | 610-612 | 3 | |
| α-helix | 615-620 | 6 | |
| α-helix | 630-632 | 3 | |
| α-helix | 635-637 | 3 | |
| β-strand | 638 | 1 | 8 |
| β-strand | 645 | 1 | 8 |
| α-helix | 651-657 | 7 | |
| α-helix | 662-664 | 3 | |
| α-helix | 668-675 | 8 | |
| α-helix | 678-687 | 10 | |
| α-helix | 689-692 | 4 | |
| α-helix | 703-715 | 13 | |
| α-helix | 720-722 | 3 | |
| α-helix | 723-727 | 5 | |
| β-strand | 730-732 | 3 | 7 |
| α-helix | 735-738 | 4 | |
| α-helix | 742-753 | 12 | |
| α-helix | 756-759 | 4 | |
| β-strand | 760 | 1 | 9 |
| α-helix | 763-780 | 18 | |
| α-helix | 789-815 | 27 | |
| α-helix | 819-822 | 4 | |
| β-strand | 824 | 1 | 9 |
| α-helix | 825-826 | 2 | |
| β-strand | 829-830 | 2 | 7 |
| α-helix | 841-850 | 10 | |
| α-helix | 853-857 | 5 | |
| β-strand | 860-861 | 2 | 2 |
| α-helix | 862-868 | 7 | |
| α-helix | 869-874 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8-11 | 4 | 10 |
| β-strand | 16-21 | 6 | 10 |
| β-strand | 29-32 | 4 | 10 |
| β-strand | 35-38 | 4 | 11 |
| β-strand | 53-54 | 2 | 11 |
| α-helix | 55-60 | 6 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 11 |
| β-strand | 71-72 | 2 | 12 |
| β-strand | 75-76 | 2 | 12 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 10 |
| α-helix | 113-127 | 15 | |
| β-strand | 131-136 | 6 | 10 |
| α-helix | 137-143 | 7 | |
| β-strand | 150-155 | 6 | 13 |
| β-strand | 160-166 | 7 | 13 |
| β-strand | 169-170 | 2 | 13 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 13 |
| α-helix | 182-194 | 13 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 14 |
| β-strand | 247-250 | 4 | 14 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-282 | 9 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 13 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 13 |
| α-helix | 338-346 | 9 | |
| β-strand | 349 | 1 | 1 |
| α-helix | 352-355 | 4 | |
| β-strand | 357-358 | 2 | 10 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-371 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13 | 1 | 15 |
| β-strand | 17-20 | 4 | 16 |
| β-strand | 25-30 | 6 | 16 |
| β-strand | 38-41 | 4 | 16 |
| β-strand | 43-47 | 5 | 17 |
| β-strand | 55-56 | 2 | 17 |
| β-strand | 69-73 | 5 | 17 |
| β-strand | 75-76 | 2 | 18 |
| β-strand | 79-80 | 2 | 18 |
| α-helix | 83-96 | 14 | |
| β-strand | 107-110 | 4 | 16 |
| α-helix | 118-125 | 8 | |
| α-helix | 126-131 | 6 | |
| β-strand | 136-139 | 4 | 16 |
| α-helix | 142-150 | 9 | |
| β-strand | 155-160 | 6 | 19 |
| β-strand | 165-171 | 7 | 19 |
| β-strand | 174-175 | 2 | 19 |
| β-strand | 181-183 | 3 | 19 |
| α-helix | 187-196 | 10 | |
| α-helix | 206-208 | 3 | |
| β-strand | 209-211 | 3 | 20 |
| β-strand | 217-218 | 2 | 20 |
| α-helix | 227-235 | 9 | |
| α-helix | 238-245 | 8 | |
| α-helix | 259-264 | 6 | |
| α-helix | 266-268 | 3 | |
| β-strand | 270-271 | 2 | 21 |
| α-helix | 276 | 1 | |
| β-strand | 277-278 | 2 | 21 |
| α-helix | 282-290 | 9 | |
| α-helix | 305-306 | 2 | |
| α-helix | 308-310 | 3 | |
| α-helix | 317-319 | 3 | |
| α-helix | 385-395 | 11 | |
| α-helix | 398-400 | 3 | |
| α-helix | 401-405 | 5 | |
| β-strand | 408-409 | 2 | 22 |
| β-strand | 410-411 | 2 | 19 |
| α-helix | 420-431 | 12 | |
| β-strand | 439-440 | 2 | 22 |
| α-helix | 447-461 | 15 | |
| α-helix | 465-468 | 4 | |
| β-strand | 471 | 1 | 16 |
| α-helix | 472-478 | 7 | |
| α-helix | 480-486 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-40 | 5 | |
| β-strand | 41-51 | 11 | 15 |
| β-strand | 57-65 | 9 | 15 |
| α-helix | 66-72 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chromatin-remodeling ATPase INO80 | G | protein | 616 | Saccharomyces cerevisiae S288C | P53115 (AlphaFold model) |
| Actin-like protein ARP8 | U | protein | 881 | Saccharomyces cerevisiae S288C | Q12386 (AlphaFold model) |
| Actin | V | protein | 375 | Saccharomyces cerevisiae S288C | P60010 (AlphaFold model) |
| Actin-related protein 4 | W | protein | 489 | Saccharomyces cerevisiae S288C | P80428 (AlphaFold model) |
| Ino eighty subunit 4 | X | protein | 116 | Saccharomyces cerevisiae S288C | Q08561 |
>8A5A_1 Chromatin-remodeling ATPase INO80 (chains G) MSLAVLLNKEDKDISDFSKTTAGKSAKKNSRERVADVAPTRVLDKKQAYLSQLNSEFNRI KRRDSIEQLYQDWKFINLQEFELISEWNQQSKDWQFDNTNDSQDLHFKKLYRDMSMINKE WAEYQSFKNANLSDIINEKDADEDEEDDEDELEDGEEDMEEDEASTGRHTNGKSMRGNGI QKSRKKDAAAAAAIGKAIKDDQTHADTVVTVNGDENEDGNNGEDEDNDNDNENNNDNDND NENENDNDSDNDDEEENGEEDEEEEEIEDLDEEDFAAFEEQDDNDDEDFNPDVEKRRKRS SSSSSSTKLSMNSLSLITSKKINKNITINSDRPKIVRELIKMCNKNKHQKIKKRRFTNCI VTDYNPIDSKLNIKITLKQYHVKRLKKLINDAKREREREEALKNNVGLDGNDLDNDEDGS ESHKRRKLNNNTANGADDANKRKFNTRHGLPTYGMKMNAKEARAIQRHYDNTYTTIWKDM ARKDSTKMSRLVQQIQSIRSTNFRKTSSLCAREAKKWQSKNFKQIKDFQTRARRGIREMS NFWKKNEREERDLKKKIEKEAMEQAKKEEEEKESKRQAKKLNFLLTQTELYSHFIGRKDY KDDDDKGTDYKDDDDK
>8A5A_2 Actin-like protein ARP8 (chains U) MSQEEAESSIIYEEPIDIPLEDDDDEDELEEENSVPLSSQADQENAENESDDSVDNVVGS ETPRSVTGLSVDPRDVADEEDEDEEGEDEDEDEDDNDVDNEDENDNDNANENENELGSSR DKRAPPAVQTSKRYKKYPKLDPAKAPPGKKVPLHLLEKRRLGRIKAAEEFAKTLKKIGIE KVETTTLPATGLFQPLMLINQKNYSSDYLKKDDQIFALRDRKFLRNNNTSQISSTNTPDV IDLKSLPHSEASAAPLNDEIDLNDPTATIVIHPGSNSIKIGFPKDDHPVVVPNCVAVPKK WLDLENSEHVENVCLQREQSEEFNNIKSEMEKNFRERMRYYKRKVPGNAHEQVVSFNENS KPEIISEKNDPSPIEWIFDDSKLYYGSDALRCVDEKFVIRKPFRGGSFNVKSPYYKSLAE LISDVTKLLEHALNSETLNVKPTKFNQYKVVLVIPDIFKKSHVETFIRVLLTELQFQAVA IIQESLATCYGAGISTSTCVVNIGAAETRIACVDEGTVLEHSAITLDYGGDDITRLFALF LLQSDFPLQDWKIDSKHGWLLAERLKKNFTTFQDADVAVQLYNFMNRSPNQPTEKYEFKL FDEVMLAPLALFFPQIFKLIRTSSHKNSSLEFQLPESRDLFTNELNDWNSLSQFESKEGN LYCDLNDDLKILNRILDAHNIIDQLQDKPENYGNTLKENFAPLEKAIVQSIANASITADV TRMNSFYSNILIVGGSSKIPALDFILTDRINIWRPSLLSSASFPQFYKKLTKEIKDLEGH YVNAPDKTEDENKQILQAQIKEKIVEELEEQHQNIEHQNGNEHIFPVSIIPPPRDMNPAL IIWKGASVLAQIKLVEELFITNSDWDVHGSRILQYKCIFTY
>8A5A_3 Actin (chains V) MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQS KRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMT QIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDL AGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSY ELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMS GGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQ EYDESGPSIVHHKCF
>8A5A_4 Actin-related protein 4 (chains W) MSNAALQVYGGDEVSAVVIDPGSYTTNIGYSGSDFPQSILPSVYGKYTADEGNKKIFSEQ SIGIPRKDYELKPIIENGLVIDWDTAQEQWQWALQNELYLNSNSGIPALLTEPVWNSTEN RKKSLEVLLEGMQFEACYLAPTSTCVSFAAGRPNCLVVDIGHDTCSVSPIVDGMTLSKST RRNFIAGKFINHLIKKALEPKEIIPLFAIKQRKPEFIKKTFDYEVDKSLYDYANNRGFFQ ECKETLCHICPTKTLEETKTELSSTAKRSIESPWNEEIVFDNETRYGFAEELFLPKEDDI PANWPRSNSGVVKTWRNDYVPLKRTKPSGVNKSDKKVTPTEEKEQEAVSKSTSPAANSAD TPNETGKRPLEEEKPPKENNELIGLADLVYSSIMSSDVDLRATLAHNVVLTGGTSSIPGL SDRLMTELNKILPSLKFRILTTGHTIERQYQSWLGGSILTSLGTFHQLWVGKKEYEEVGV ERLLNDRFR
>8A5A_5 Ino eighty subunit 4 (chains X) MSQESSVLSESQEQLANNPKIEDTSPPSANSRDNSKPVLPWDYKNKAIEIKSFSGYKVNF TGWIRRDVREERQRGSEFTASDVKGSDDKATRKKEPADEDPEVKQLEKEGEDGLDS
Structural mechanism of extranucleosomal DNA readout by the INO80 complex. Kunert, F., Metzner, F.J., Jung, J. et al. Sci Adv (2022) 8:eadd3189-eadd3189. DOI 10.1126/sciadv.add3189 · PubMed
Other PDB entries of the same protein (UniProt P53115 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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