9HHL: Dynein-Dynactin-NuMA-LIS1

Structure of Dynein-Dynactin-NuMA-LIS1. Determined by electron microscopy at 6.53 Å resolution. Released 3 Dec 2025.

Method: Electron microscopy
Resolution: 6.53 Å
Organisms: Homo sapiens, Sus scrofa
Chains: 41
Atoms: 64,583
Mol. weight: 3953.07 kDa
Ligands: ZN, ATP, ADP
Released: 3 Dec 2025

Explore 9HHL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9HHL contains 568 α-helices and 530 β-strands across 41 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 1: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	212-263	52
α-helix	277-394	118
β-strand	407-408	2	17
α-helix	409-424	16

Chain 2: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	212-264	53
α-helix	277-394	118
α-helix	409-424	16

Chain A: 20 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	10-11	2
β-strand	12-16	5	28
β-strand	20-25	6	28
β-strand	35-36	2	28
β-strand	39-42	4	29
β-strand	45-46	2	30
β-strand	57	1	29
α-helix	60-64	5
β-strand	69-72	4	29
β-strand	75-76	2	31
β-strand	79-80	2	31
α-helix	83-92	10
β-strand	108-112	5	28
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-141	6	28
α-helix	142-149	8
β-strand	155-160	6	32
β-strand	165-171	7	32
β-strand	174-175	2	32
β-strand	181-183	3	32
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	33
α-helix	228-233	6
β-strand	240-242	3	34
β-strand	248-250	3	34
α-helix	254-257	4
α-helix	259-261	3
α-helix	265-267	3
α-helix	275-283	9
α-helix	288-296	9
β-strand	298-301	4	32
α-helix	304-306	3
β-strand	308	1	33
α-helix	310-319	10
β-strand	330-331	2	32
α-helix	339-348	10
α-helix	352-354	3
β-strand	358-359	2	28
α-helix	360-365	6
α-helix	368-374	7

Chain B: 22 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	12-16	5	39
β-strand	20-25	6	39
β-strand	33-36	4	39
β-strand	39-42	4	40
β-strand	45-46	2	41
β-strand	57	1	40
α-helix	60-64	5
α-helix	66-68	3
β-strand	69-72	4	40
β-strand	75-76	2	42
β-strand	79-80	2	42
α-helix	83-93	11
α-helix	103-105	3
β-strand	108-112	5	39
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-141	6	39
α-helix	142-150	9
β-strand	155-160	6	43
β-strand	165-171	7	43
β-strand	174-175	2	43
β-strand	181-183	3	43
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	44
α-helix	228-233	6
α-helix	235-236	2
β-strand	240-242	3	45
β-strand	248-250	3	45
α-helix	254-257	4
α-helix	258-262	5
α-helix	265-268	4
α-helix	275-284	10
α-helix	288-295	8
β-strand	298-301	4	43
α-helix	303-306	4
β-strand	308	1	44
α-helix	311-321	11
β-strand	328-331	4	43
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	39
α-helix	360-366	7
α-helix	368-374	7

Chain C: 22 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	10-11	2
β-strand	12-16	5	113
β-strand	20-25	6	113
β-strand	33-36	4	113
β-strand	39-42	4	114
β-strand	45-46	2	69
β-strand	57-58	2	114
α-helix	60-64	5
β-strand	69-72	4	114
β-strand	75-76	2	115
β-strand	79-80	2	115
α-helix	83-93	11
β-strand	108-111	4	113
α-helix	112-113	2
α-helix	119-126	8
α-helix	127-131	5
β-strand	136-140	5	113
α-helix	142-150	9
β-strand	155-160	6	30
β-strand	165-171	7	30
β-strand	174-175	2	30
β-strand	181-183	3	30
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	116
α-helix	228-232	5
β-strand	240-242	3	117
β-strand	248-250	3	117
α-helix	254-257	4
α-helix	258-260	3
α-helix	265-267	3
α-helix	275-284	10
α-helix	291-296	6
β-strand	298-301	4	30
α-helix	303-305	3
β-strand	308	1	116
α-helix	310-321	12
α-helix	323	1
β-strand	330-333	4	30
α-helix	339-348	10
α-helix	353-356	4
β-strand	358-359	2	113
α-helix	360-366	7
α-helix	369-372	4

Chain D: 19 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	12-15	4	49
β-strand	20-25	6	49
β-strand	33-36	4	49
β-strand	39-42	4	50
β-strand	45-46	2	51
β-strand	57	1	50
α-helix	60-64	5
β-strand	69-72	4	50
β-strand	75-76	2	52
β-strand	79-80	2	52
α-helix	83-93	11
β-strand	108-111	4	49
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-140	5	49
α-helix	142-150	9
β-strand	156-160	5	53
β-strand	165-168	4	53
β-strand	170-171	2	41
β-strand	174-175	2	41
β-strand	181-183	3	53
α-helix	187-201	15
α-helix	208-221	14
β-strand	223	1	54
β-strand	240-242	3	55
β-strand	248-250	3	55
α-helix	254-257	4
α-helix	259-261	3
α-helix	265-267	3
α-helix	275-285	11
α-helix	291-296	6
β-strand	297-301	5	53
α-helix	303-306	4
β-strand	308	1	54
α-helix	310-321	12
α-helix	323	1
β-strand	329-331	3	53
α-helix	339-348	10
α-helix	353-356	4
β-strand	358-359	2	49
α-helix	360-366	7
α-helix	368-375	8

Chain e: 39 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	22-23	2
β-strand	24	1	135
α-helix	25-26	2
α-helix	27-37	11
α-helix	39-42	4
α-helix	50-56	7
α-helix	59-70	12
β-strand	76-86	11	136
α-helix	93-95	3
β-strand	96-104	9	136
β-strand	113-120	8	136
β-strand	126	1	135
β-strand	135-140	6	136
α-helix	145-152	8
α-helix	153-157	5
α-helix	158-168	11
α-helix	179-198	20
α-helix	201-204	4
α-helix	211-222	12
α-helix	229-232	4
α-helix	235-237	3
α-helix	239-260	22
α-helix	271-292	22
α-helix	295-306	12
α-helix	310-314	5
α-helix	315-319	5
α-helix	322-336	15
α-helix	341-345	5
α-helix	350-364	15
α-helix	374-399	26
α-helix	406-440	35
α-helix	457-483	27
α-helix	514-529	16
α-helix	540-572	33
α-helix	578-587	10
α-helix	597-624	28
α-helix	631-638	8
α-helix	643-669	27
α-helix	673-675	3
α-helix	677-691	15
α-helix	696-709	14
β-strand	718	1	137
β-strand	721-723	3	138
β-strand	732-734	3	138
β-strand	737	1	137
α-helix	741-756	16
α-helix	762-797	36
α-helix	806-820	15
α-helix	829-848	20

Chain E: 23 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	10-11	2
β-strand	12-15	4	64
β-strand	20-25	6	64
β-strand	33-36	4	64
β-strand	39-42	4	65
α-helix	45	1
β-strand	46	1	66
β-strand	57	1	65
α-helix	60-64	5
β-strand	69-72	4	65
β-strand	75-76	2	67
β-strand	79-80	2	67
α-helix	83-93	11
β-strand	108-111	4	64
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-140	5	64
α-helix	142-150	9
β-strand	155-160	6	68
β-strand	165-170	6	68
β-strand	171	1	69
β-strand	174-175	2	69
β-strand	181-183	3	68
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	70
α-helix	228-233	6
α-helix	235-237	3
β-strand	240-242	3	71
β-strand	248-250	3	71
α-helix	254-257	4
α-helix	258-261	4
α-helix	265-268	4
α-helix	275-285	11
α-helix	291-296	6
β-strand	298-301	4	68
α-helix	303-305	3
β-strand	308	1	70
α-helix	310-321	12
α-helix	323	1
β-strand	329-331	3	68
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	64
α-helix	360-366	7
α-helix	368-374	7

33 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
Cytoplasmic dynein 1 intermediate chain 2	g, h, o, p	protein	612	Homo sapiens	Q13409 (AlphaFold model)
Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase	1, 2	protein	889	Homo sapiens	P16455 (AlphaFold model), Q14980 (AlphaFold model)
ARP1 actin related protein 1 homolog A	A, B, C, D, E, F, G, I	protein	376	Sus scrofa	F2Z5G5 (AlphaFold model)
Actin, cytoplasmic 1	H	protein	375	Sus scrofa	Q6QAQ1
Arp11	J	protein	417	Sus scrofa	I3LHK5
Capping protein (Actin filament) muscle Z-line, alpha 1	K	protein	286	Sus scrofa	A0PFK5
F-actin-capping protein subunit beta	L	protein	272	Sus scrofa	A0PFK7
Dynactin subunit 2	M, N, P, Q, V	protein	405	Sus scrofa	A0A5G2QD80
Dynactin subunit 3	O, R	protein	186	Sus scrofa	F1SEC0
Dynactin 6	U	protein	190	Sus scrofa	D0G6S1
Dynactin subunit 5	W	protein	182	Sus scrofa	A0A286ZK88
Dynactin subunit 4	Y	protein	467	Sus scrofa	A0A4X1TB62

4 more molecules are not listed.

Sequence of entity 1 (g, h, o, p), FASTA

>9HHL_1 Cytoplasmic dynein 1 intermediate chain 2 (chains g, h, o, p)
MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREA
EALLQSMGLTPESPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQV
DFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPH
ELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLS
LNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPE
YVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYC
VNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNN
FVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTV
KLWSTKNNKPLYSFEDNAGYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASIS
VEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRA
DAEEEAATRIPA

Sequence of entity 2 (1, 2), FASTA

>9HHL_2 Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase (chains 1, 2)
MTLHATRGAALLSWVNSLHVADPVEAVLQLQDCSIFIKIIDRIHGTEEGQQILKQPVSER
LDFVCSFLQKNRKHPSSPECLVSAQKVLEGSELELAKMTMLLLYHSTMSSKSPRDWEQFE
YKIQAELAVILKFVLDHEDGLNLNEDLENFLQKAPVPSTCSSTFPEELSPPSHQAKREIR
FLELQKVASSSSGNNFLSGSPASPMGDILQTPQFQMRRLKKQLADERSNRDELELELAEN
RKLLTEKDAQIAMMQQRIDRLALLNEKQAASPLEPKELEELRDKNESLTMRLHETLKQCQ
DLKTEKSQMDRKINQLSEENGDLSFKLREFASHLQQLQDALNELTEEHSKATQEWLEKQA
QLEKELSAALQDKKCLEEKNEILQGKLSQLEEHLSQLQDNPPQEKGEVLGDVLQLETLKQ
EAATLAANNTQLQARVEMLETERGQQEAKLLAERGHFEEEKQQLSSLITDLQSSISNLSQ
AKEELEQASQAHGARLTAQVASLTSELTTLNATIQQQDQELAGLKQQAKEKQAQLAQTLQ
QQEQASQGLRHQVEQLSSSLKQKEQQLKEVAEKQEATRQDHAQQLATAAEEREASLRERD
AALKQLEALEKEKAAKLEILQQQLQVANEARDSAQTSVTQAQREKAELSRKVEELQACVE
TARQEQHEAQAQVAELELQLRSEQQKATEKERVAQEKDQLQEQLQGSMDKDCEMKRTTLD
SPLGKLELSGCEQGLHRIIFLGKGTSAADAVEVPAPAAVLGGPEPLMQATAWLNAYFHQP
EAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYSHLAALAGNPAATAAVKTA
LSGNPVPILIPCHRVVQGDLDVGGYEGGLAVKEWLLAHEGHRLGKPGLG

Sequence of entity 3 (A, B, C, D, E, F, G, I), FASTA

>9HHL_3 ARP1 actin related protein 1 homolog A (chains A, B, C, D, E, F, G, I)
MESYDVIANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHVRVMAGALEGDIFIGP
KAEEHRGLLSIRYPMEHGIVKDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPRKN
RERAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSI
MRIDIAGRDVSRFLRLYLRKEGYDFHSSSEFEIVKAIKERACYLSINPQKDETLETEKAQ
YYLPDGSTIEIGPSRFRAPELLFRPDLIGEESEGIHEVLVFAIQKSDMDLRRTLFSNIVL
SGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPQERLYSTWIGGSILASLDTFKKMWVSK
KEYEEDGARSIHRKTF

Sequence of entity 4 (H), FASTA

>9HHL_4 Actin, cytoplasmic 1 (chains H)
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT
QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL
AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ
EYDESGPSIVHRKCF

Sequence of entity 5 (J), FASTA

>9HHL_5 Arp11 (chains J)
MPLYEGLGSGGEKTAVVIDLGEAFTKCGFAGETGPRCIIPSVIKKAGMPKPIKVVQYNIN
TEELYSYLKEFIHILYFRHLLVNPRDRRVVVIESVLCPSHFRETLTRVLFKYFEVPSVLL
APSHLMALLTLGINSAMVLDCGYRESLVLPIYEGIPVLNCWGALPLGGKALHKELETQLL
EQCTVDTGAAKEQSLPSVMGSIPEGVLEDIKVRTCFVSDLTRGLKIQAAKFNIDGNTERP
SPPPNVDYPLDGEKILHVLGSIRDSVVEILFEQDNEEKSVATLILDSLMQCPIDTRKQLA
ENLVIIGGTSMLPGFLHRLLAEIRYLVEKPKYKKTLGTKTFRIHTPPAKANCVAWLGGAI
FGALQDILGSRSVSKEYYNQTGRIPDWCSLNNPPLEMVFDVGKSQPPLMKRAFSTEK

Sequence of entity 6 (K), FASTA

>9HHL_6 Capping protein (Actin filament) muscle Z-line, alpha 1 (chains K)
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEVDGSLKSW
RESCDSALRAYVKDHYSNGFCTVYAKNIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSVTVSNEAQTAKEFIKIIEHAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA

Sequence of entity 7 (L), FASTA

>9HHL_7 F-actin-capping protein subunit beta (chains L)
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN
KSGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV
NGLRSVQTFADKSKQEALKNDLVEALKRKQQC

Sequence of entity 8 (M, N, P, Q, V), FASTA

>9HHL_8 Dynactin subunit 2 (chains M, N, P, Q, V)
MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAELEELTSTSVEHIIVNPNAAYDKFK
DKRVGTKGLDFSDRIGKTKRTGYESGEYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVE
KIKMTVKESATEEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAINLTDPDGALAKRLL
LQLEATKNTKGAGSGGKTTSGSPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEA
TVRCDQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKH
KASVEDADTQSKVHQLYETIQRWSPIASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTT
QQMIACSLKDNATLLTQVQTTMRENLSTVEGNFANIDERMKKLGK

Sequence of entity 9 (O, R), FASTA

>9HHL_9 Dynactin subunit 3 (chains O, R)
MAGVTDVQRLQARLEELERWVYGPGGSRGSRKVADGLVKVQVALGNIASKRERVKILYKK
IEDLIKYLDPEYMDRIAIPDASKLQFILAEEQFILSQVALLEQVEALVPMLDSAHIKAVP
EHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAAKQ
VKPAEE

Sequence of entity 10 (U), FASTA

>9HHL_10 Dynactin 6 (chains U)
MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQA
LIINAHPDNITPDAEDSEPKPMIIGTNNVFEVGCYSQAMKMGDNNVIESKAYVGRNVILT
SGCIIGACCNLNTFEVIPENTVIYGADCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKT
MKGSSTPVKN

Sequence of entity 11 (W), FASTA

>9HHL_11 Dynactin subunit 5 (chains W)
MELGELLYNKSEYIETASGNKVSRQSVLCGSQNIVLNGKTIVMNDCIIRGDLANVRVGRH
CVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRC
VLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSYYQKFLPLT
QV

Sequence of entity 12 (Y), FASTA

>9HHL_12 Dynactin subunit 4 (chains Y)
MASLLQSERVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPS
AEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTAVKKAYYLACGFCRWTSRD
VGMADKSVASGGWQEPDHPHTQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSQ
HTIHVVDKYGLGTRLQRPRAGTTITALAGLSLKEGEDQKEIKIEPAQAVDEVEPLPEDYY
TRPVNLTEVTTLQQRLLQPDFQPICASQLYPRHKHLLIKRSLRCRQCEHNLSKPEFNPTS
IKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLLECEEGDPDDTN
STAKVSVPPTELVLAGKDAAAEYDELAEPQDFPDDPDVVAFRKANKVGVFIKVTPQREEG
DVTVCFKLKHDFKNLAAPIRPVEEADPGAEVSWLTQHVELSLGPLLP

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	3
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	8

Primary citation

Activation and regulation of the dynein-dynactin-NuMA complex. Aslan, M., d'Amico, E.A., Cho, N.H. et al. Nat Chem Biol (2026) 22:1434-1445. DOI 10.1038/s41589-026-02156-7 · PubMed

Other PDB entries of the same protein (UniProt Q13409 (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,…
6F1U 3.4 Å, N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1
6F1Z 3.4 Å, Roadblock-1 region of the dynein tail/dynactin/BICDR1 complex
6F1T 3.5 Å, Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1
9BLY 3.5 Å, Composite structure of full-length human dynein-1 in phi-particle conformation
8PR2 3.8 Å, Cytoplasmic dynein-1 heavy chain bound to JIP3-LZI
8PR3 3.9 Å, Cytoplasmic dynein-1 heavy chain bound to JIP3-RH1
7Z8J 3.93 Å, Cytoplasmic dynein (A2) bound to BICDR1
9YNC 3.93 Å, Motor domains of phi-like human dynein-1 bound to dynactin-p150glued and LIS1
9YNG 4.07 Å, Dynactin and dynein-1 tail region of dynein-dynactin complex on microtubule in the…
8PQW 4.2 Å, Cytoplasmic dynein-1 motor domain bound to dynactin-p150glued and LIS1
9YND 4.26 Å, Motor domain of human dynein-1 in pre-power stroke bound to dynactin-p150glued-CC1B and…

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