6F1U: N terminal region of dynein tail domains
N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1. Determined by electron microscopy at 3.4 Å resolution. Released 17 Jan 2018.
- Method
- Electron microscopy
- Resolution
- 3.4 Å
- Organisms
- Sus scrofa, Homo sapiens, Mus musculus
- Chains
- 13
- Atoms
- 28,866
- Mol. weight
- 810.94 kDa
- Ligands
- ADP
- Released
- 17 Jan 2018
Explore 6F1U in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6F1U contains 157 α-helices and 141 β-strands across 13 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: 19 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-15 | 4 | 1 |
| β-strand | 20-25 | 6 | 1 |
| β-strand | 33-36 | 4 | 1 |
| β-strand | 39 | 1 | 2 |
| β-strand | 40 | 1 | 3 |
| β-strand | 42 | 1 | 4 |
| β-strand | 45-46 | 2 | 5 |
| β-strand | 57 | 1 | 3 |
| α-helix | 60-64 | 5 | |
| β-strand | 69 | 1 | 4 |
| β-strand | 72 | 1 | 2 |
| β-strand | 75-76 | 2 | 6 |
| β-strand | 79-80 | 2 | 6 |
| α-helix | 83-93 | 11 | |
| β-strand | 108-111 | 4 | 1 |
| α-helix | 118-126 | 9 | |
| α-helix | 127-132 | 6 | |
| β-strand | 136-140 | 5 | 1 |
| α-helix | 143-150 | 8 | |
| β-strand | 155-160 | 6 | 7 |
| β-strand | 165-171 | 7 | 7 |
| β-strand | 174-175 | 2 | 7 |
| β-strand | 181-183 | 3 | 7 |
| α-helix | 187-201 | 15 | |
| α-helix | 211-221 | 11 | |
| β-strand | 223 | 1 | 8 |
| β-strand | 242 | 1 | 9 |
| β-strand | 248 | 1 | 9 |
| α-helix | 252-255 | 4 | |
| α-helix | 259-263 | 5 | |
| α-helix | 275-284 | 10 | |
| α-helix | 288-290 | 3 | |
| α-helix | 291-295 | 5 | |
| β-strand | 298-301 | 4 | 7 |
| α-helix | 303-306 | 4 | |
| β-strand | 308 | 1 | 8 |
| α-helix | 310-321 | 12 | |
| α-helix | 323 | 1 | |
| β-strand | 328-331 | 4 | 7 |
| α-helix | 339-348 | 10 | |
| α-helix | 353-356 | 4 | |
| β-strand | 358-359 | 2 | 1 |
| α-helix | 360-365 | 6 | |
| α-helix | 368-373 | 6 | |
Chain c: 1 helix, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-8 | 6 | |
| β-strand | 19-21 | 3 | 5 |
| β-strand | 45-47 | 3 | 7 |
Chain d: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-6 | 3 | |
| β-strand | 19-21 | 3 | 12 |
Chain D: 20 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-15 | 4 | 10 |
| β-strand | 20-25 | 6 | 10 |
| β-strand | 33-36 | 4 | 10 |
| β-strand | 39-42 | 4 | 11 |
| β-strand | 46 | 1 | 12 |
| β-strand | 57 | 1 | 11 |
| α-helix | 61-63 | 3 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-72 | 4 | 11 |
| β-strand | 75-76 | 2 | 13 |
| β-strand | 79-80 | 2 | 13 |
| α-helix | 83-93 | 11 | |
| β-strand | 108-110 | 3 | 10 |
| α-helix | 118-126 | 9 | |
| α-helix | 127-131 | 5 | |
| β-strand | 136-139 | 4 | 10 |
| α-helix | 144-148 | 5 | |
| β-strand | 155-160 | 6 | 5 |
| β-strand | 165-171 | 7 | 5 |
| β-strand | 174-175 | 2 | 5 |
| α-helix | 177-179 | 3 | |
| β-strand | 181-183 | 3 | 5 |
| α-helix | 187-200 | 14 | |
| α-helix | 211-221 | 11 | |
| β-strand | 223 | 1 | 14 |
| β-strand | 240-242 | 3 | 15 |
| β-strand | 248-250 | 3 | 15 |
| α-helix | 259-261 | 3 | |
| α-helix | 275-284 | 10 | |
| α-helix | 288-290 | 3 | |
| α-helix | 291-295 | 5 | |
| β-strand | 298-301 | 4 | 5 |
| α-helix | 303-306 | 4 | |
| β-strand | 308 | 1 | 14 |
| α-helix | 310-321 | 12 | |
| α-helix | 323 | 1 | |
| β-strand | 329-331 | 3 | 5 |
| α-helix | 339-347 | 9 | |
| α-helix | 352-356 | 5 | |
| β-strand | 358-359 | 2 | 10 |
| α-helix | 360-365 | 6 | |
| α-helix | 368-373 | 6 | |
Chain f: 29 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 211-222 | 12 | |
| α-helix | 233-235 | 3 | |
| α-helix | 239-260 | 22 | |
| α-helix | 271-293 | 23 | |
| α-helix | 295-306 | 12 | |
| α-helix | 310-318 | 9 | |
| α-helix | 322-332 | 11 | |
| α-helix | 342-345 | 4 | |
| α-helix | 350-363 | 14 | |
| α-helix | 374-397 | 24 | |
| α-helix | 406-440 | 35 | |
| α-helix | 455-482 | 28 | |
| α-helix | 519-533 | 15 | |
| α-helix | 539-541 | 3 | |
| α-helix | 542 | 1 | |
| α-helix | 543-547 | 5 | |
| α-helix | 548-574 | 27 | |
| α-helix | 578-587 | 10 | |
| α-helix | 590-593 | 4 | |
| α-helix | 597-603 | 7 | |
| α-helix | 605-624 | 20 | |
| α-helix | 631-638 | 8 | |
| α-helix | 643-669 | 27 | |
| α-helix | 679-692 | 14 | |
| α-helix | 696-706 | 11 | |
| β-strand | 722 | 1 | 31 |
| β-strand | 726 | 1 | 32 |
| β-strand | 732 | 1 | 32 |
| β-strand | 736 | 1 | 31 |
| α-helix | 742-755 | 14 | |
| α-helix | 762-772 | 11 | |
| α-helix | 775-796 | 22 | |
| α-helix | 801-821 | 21 | |
Chain F: 22 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-15 | 4 | 16 |
| β-strand | 20-25 | 6 | 16 |
| β-strand | 33-36 | 4 | 16 |
| β-strand | 39-42 | 4 | 17 |
| α-helix | 60-64 | 5 | |
| β-strand | 69-72 | 4 | 17 |
| β-strand | 75-76 | 2 | 18 |
| β-strand | 79-80 | 2 | 18 |
| α-helix | 83-93 | 11 | |
| β-strand | 108-112 | 5 | 16 |
| α-helix | 118-126 | 9 | |
| α-helix | 127-131 | 5 | |
| β-strand | 136-141 | 6 | 16 |
| α-helix | 142-149 | 8 | |
| β-strand | 155-160 | 6 | 12 |
| β-strand | 165-171 | 7 | 12 |
| β-strand | 174-175 | 2 | 12 |
| α-helix | 177-179 | 3 | |
| β-strand | 181-183 | 3 | 12 |
| α-helix | 187-200 | 14 | |
| α-helix | 208-220 | 13 | |
| β-strand | 223 | 1 | 19 |
| α-helix | 228-232 | 5 | |
| β-strand | 240-242 | 3 | 20 |
| α-helix | 243 | 1 | |
| β-strand | 248-250 | 3 | 20 |
| α-helix | 254-257 | 4 | |
| α-helix | 258-260 | 3 | |
| α-helix | 275-284 | 10 | |
| α-helix | 291-295 | 5 | |
| β-strand | 298-301 | 4 | 12 |
| α-helix | 303-305 | 3 | |
| β-strand | 308 | 1 | 19 |
| α-helix | 310-321 | 12 | |
| α-helix | 323 | 1 | |
| β-strand | 329-331 | 3 | 12 |
| α-helix | 336-338 | 3 | |
| α-helix | 339-348 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 358-359 | 2 | 16 |
| α-helix | 360-366 | 7 | |
| α-helix | 368-373 | 6 | |
Chain h: 4 helices, 33 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 244-245 | 2 | 33 |
| β-strand | 259-260 | 2 | 34 |
| β-strand | 270-271 | 2 | 34 |
| β-strand | 286-289 | 4 | 34 |
| α-helix | 292-294 | 3 | |
| β-strand | 301-304 | 4 | 34 |
| β-strand | 311-314 | 4 | 35 |
| β-strand | 321-325 | 5 | 35 |
| β-strand | 332-335 | 4 | 35 |
| α-helix | 346-348 | 3 | |
| β-strand | 358-363 | 6 | 36 |
| β-strand | 372-376 | 5 | 36 |
| β-strand | 380-384 | 5 | 36 |
| β-strand | 394-397 | 4 | 36 |
| β-strand | 399 | 1 | 37 |
| β-strand | 405 | 1 | 37 |
| β-strand | 412 | 1 | 38 |
| β-strand | 421-423 | 3 | 38 |
| β-strand | 427 | 1 | 39 |
| β-strand | 430-434 | 5 | 38 |
| β-strand | 441-446 | 6 | 38 |
| β-strand | 452 | 1 | 39 |
| β-strand | 453-457 | 5 | 40 |
| β-strand | 471-475 | 5 | 40 |
| β-strand | 479-480 | 2 | 41 |
| β-strand | 482-483 | 2 | 40 |
| β-strand | 494-495 | 2 | 41 |
| β-strand | 504-506 | 3 | 42 |
| β-strand | 514-516 | 3 | 42 |
| β-strand | 522-523 | 2 | 43 |
| β-strand | 524-526 | 3 | 42 |
| β-strand | 539-540 | 2 | 43 |
| β-strand | 549-552 | 4 | 33 |
| α-helix | 553 | 1 | |
| β-strand | 559-562 | 4 | 33 |
| β-strand | 568-571 | 4 | 33 |
| α-helix | 584-593 | 10 | |
Chain K: 12 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-21 | 11 | |
| α-helix | 24-25 | 2 | |
| α-helix | 29-40 | 12 | |
| α-helix | 43-60 | 18 | |
| β-strand | 63-64 | 2 | 21 |
| β-strand | 75-76 | 2 | 21 |
| β-strand | 87-89 | 3 | 22 |
| α-helix | 91-93 | 3 | |
| β-strand | 94-96 | 3 | 22 |
| β-strand | 97-99 | 3 | 23 |
| β-strand | 104-106 | 3 | 23 |
| α-helix | 118-135 | 18 | |
| β-strand | 136 | 1 | 24 |
| β-strand | 140-146 | 7 | 25 |
| α-helix | 148-150 | 3 | |
| β-strand | 152-161 | 10 | 25 |
| β-strand | 164 | 1 | 25 |
| α-helix | 165-167 | 3 | |
| β-strand | 169 | 1 | 25 |
| β-strand | 172-181 | 10 | 25 |
| β-strand | 186-191 | 6 | 25 |
| β-strand | 194-198 | 5 | 25 |
| β-strand | 203 | 1 | 26 |
| β-strand | 204-209 | 6 | 25 |
| β-strand | 211-216 | 6 | 25 |
| α-helix | 222-248 | 27 | |
| α-helix | 250-254 | 5 | |
| α-helix | 255-258 | 4 | |
| α-helix | 271-276 | 6 | |
5 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| ARP1 actin related protein 1 homolog A | B, D, F | protein | 376 | Sus scrofa | F2Z5G5 (AlphaFold model) |
| Capping protein (Actin filament) muscle Z-line, alpha 1 | K | protein | 286 | Sus scrofa | A0PFK5 (AlphaFold model) |
| F-actin capping protein beta subunit | L | protein | 271 | Sus scrofa | A0PFK7 (AlphaFold model) |
| Dynactin subunit 2 | c | protein | 50 | Sus scrofa | A0A5G2QD80 (AlphaFold model) |
| Dynactin subunit 2 | d | protein | 26 | Sus scrofa | A0A5G2QD80 (AlphaFold model) |
| Cytoplasmic dynein 1 heavy chain 1 | f, m, n | protein | 1186 | Homo sapiens | Q14204 |
| Cytoplasmic dynein 1 intermediate chain 2 | h | protein | 612 | Homo sapiens | Q13409 |
| BICD family-like cargo adapter 1 | X, x | protein | 577 | Mus musculus | A0JNT9 |
Sequence of entity 1 (B, D, F), FASTA
>6F1U_1 ARP1 actin related protein 1 homolog A (chains B, D, F)
MESYDVIANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHVRVMAGALEGDIFIGP
KAEEHRGLLSIRYPMEHGIVKDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPRKN
RERAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSI
MRIDIAGRDVSRFLRLYLRKEGYDFHSSSEFEIVKAIKERACYLSINPQKDETLETEKAQ
YYLPDGSTIEIGPSRFRAPELLFRPDLIGEESEGIHEVLVFAIQKSDMDLRRTLFSNIVL
SGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPQERLYSTWIGGSILASLDTFKKMWVSK
KEYEEDGARSIHRKTF
Sequence of entity 2 (K), FASTA
>6F1U_2 Capping protein (Actin filament) muscle Z-line, alpha 1 (chains K)
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEVDGSLKSW
RESCDSALRAYVKDHYSNGFCTVYAKNIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSVTVSNEAQTAKEFIKIIEHAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
Sequence of entity 3 (L), FASTA
>6F1U_3 F-actin capping protein beta subunit (chains L)
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN
KSGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV
NGLRSVQTFADKSKQEALKNDLVEALKRKQQ
Sequence of entity 4 (c), FASTA
>6F1U_4 Dynactin subunit 2 (chains c)
MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDALQEELTSTSVEHIIV
Sequence of entity 5 (d), FASTA
>6F1U_5 Dynactin subunit 2 (chains d)
MADPKYADLPGIARNEPDVYETSDLP
Sequence of entity 6 (f, m, n), FASTA
>6F1U_6 Cytoplasmic dynein 1 heavy chain 1 (chains f, m, n)
MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKS
ALEQMRKFLSDPQVHTVLVERSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIK
RTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPFFKSYIRESGKADRDGDKMAP
SVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLT
LDILKHGKRFHATVSFDTDTGLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAI
FTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRKLMHVAYEEFEKVMVACFEVF
QTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSK
EGTEAWEAAMKRYDERIDRVETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGA
IREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRDLPPVSGSIIWAKQIDRQLTA
YMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAIS
LIESVRTYERTCEKVEERNTISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETV
FNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNRVQKAVDDLNLHSYSNLPIWV
NKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYR
NALTRMPDGPVALEESYSAVMGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQ
ALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKYDSWHKEVLSKFGQMLGSNMT
EFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQ
Sequence of entity 7 (h), FASTA
>6F1U_7 Cytoplasmic dynein 1 intermediate chain 2 (chains h)
MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREA
EALLQSMGLTPESPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQV
DFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPH
ELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLS
LNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPE
YVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYC
VNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNN
FVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTV
KLWSTKNNKPLYSFEDNAGYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASIS
VEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRA
DAEEEAATRIPA
Sequence of entity 8 (X, x), FASTA
>6F1U_8 BICD family-like cargo adapter 1 (chains X, x)
MSAFCLGLAGRASAPAEPDSACCMELPAGAGDAVRSPATAAALVSFPGGPGELELALEEE
LALLAAGERSSEPGEHPQAEPESPVEGHGPPLPPPPTQDPELLSVIRQKEKDLVLAARLG
KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQL
QDELERQQLHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREK
NSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQG
HDKDLQLHQSQLELQEVRLSYRQLQGKVEELTEERSLQSSAATSTSLLSEIEQSMEAEEL
EQEREQLRLQLWEAYCQVRYLCSHLRGNDSADSAVSTDSSMDESSETSSAKDVPAGSLRT
ALNDLKRLIQSIVDGVEPTVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEA
IAKKNAVELELAKCKMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQLMDTHLK
EQSRPAAAAFPRGHGVGRGQEPSTADGKRLFSFFRKI
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 3 |
Primary citation
Cryo-EM shows how dynactin recruits two dyneins for faster movement. Urnavicius, L., Lau, C.K., Elshenawy, M.M. et al. Nature (2018) 554:202-206. DOI 10.1038/nature25462 · PubMed
Other PDB entries of the same protein (UniProt F2Z5G5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7Z8I 3.3 Å, The barbed end complex of dynactin bound to BICDR1 and the cytoplasmic dynein tails (A2,…
- 6F1T 3.5 Å, Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1
- 6ZNL 3.8 Å, Cryo-EM structure of the dynactin complex
- 5ADX 4.0 Å, CryoEM structure of dynactin complex at 4.0 angstrom resolution
- 6ZNM 4.1 Å, The pointed end complex of dynactin bound to BICDR1
- 7Z8K 4.37 Å, Cytoplasmic dynein (A1) bound to BICDR1
- 6ZNN 4.5 Å, The pointed end complex of dynactin bound to Hook3
- 9HHL 6.53 Å, Structure of Dynein-Dynactin-NuMA-LIS1
- 6F38 6.7 Å, Cryo-EM structure of two dynein tail domains bound to dynactin and HOOK3
- 6ZNO 6.8 Å, The pointed end complex of dynactin with the p150 projection docked
- 5AFU 8.2 Å, Cryo-EM structure of dynein tail-dynactin-BICD2N complex
- 6F3A 8.2 Å, Cryo-EM structure of a single dynein tail domain bound to dynactin and BICD2N
Browse structure collections
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