5ADX: Dynactin complex

CryoEM structure of dynactin complex at 4.0 angstrom resolution. Determined by electron microscopy at 4.0 Å resolution. Released 30 Dec 2015.

Method: Electron microscopy
Resolution: 4.0 Å
Organism: SUS SCROFA
Chains: 27
Atoms: 49,392
Mol. weight: 805.39 kDa
Released: 30 Dec 2015

Explore 5ADX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5ADX contains 309 α-helices and 319 β-strands across 27 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 a: 2 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	13-15	3	22
α-helix	16-19	4
β-strand	47	1	26
α-helix	52-60	9

Chain A: 21 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	12-14	3	1
β-strand	15	1	2
β-strand	20-23	4	2
β-strand	25	1	1
β-strand	33-36	4	2
β-strand	39-42	4	3
β-strand	45	1	4
β-strand	57	1	3
α-helix	60-64	5
β-strand	69-72	4	3
β-strand	75-76	2	5
β-strand	79-80	2	5
α-helix	83-94	12
β-strand	108-111	4	1
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-140	5	1
α-helix	142-150	9
β-strand	155-160	6	6
β-strand	165-170	6	6
β-strand	175	1	6
β-strand	181-183	3	6
α-helix	187-201	15
α-helix	211-220	10
β-strand	223	1	7
α-helix	228-233	6
α-helix	235-236	2
β-strand	240-242	3	8
β-strand	248-250	3	8
α-helix	254-257	4
α-helix	259-262	4
α-helix	275-285	11
α-helix	288-290	3
α-helix	291-296	6
β-strand	298-299	2	6
α-helix	303-305	3
β-strand	308	1	7
α-helix	310-321	12
α-helix	323	1
β-strand	330-331	2	6
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	1
α-helix	360-365	6
α-helix	368-375	8

Chain b: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	13-15	3	51
α-helix	16-19	4
β-strand	47	1	55
α-helix	52-60	9
β-strand	64	1	93
β-strand	86	1	93

Chain B: 20 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	12-14	3	9
β-strand	15	1	10
β-strand	20-23	4	10
β-strand	25	1	9
β-strand	33-36	4	10
β-strand	39	1	11
β-strand	40	1	12
β-strand	42	1	13
β-strand	45	1	14
β-strand	57	1	12
α-helix	60-64	5
β-strand	69	1	13
β-strand	72	1	11
β-strand	75-76	2	15
β-strand	79-80	2	15
α-helix	83-94	12
β-strand	108-111	4	9
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-140	5	9
α-helix	142-150	9
β-strand	155-159	5	16
β-strand	165-170	6	16
β-strand	175	1	16
β-strand	181-183	3	16
α-helix	187-201	15
α-helix	211-220	10
β-strand	223	1	17
α-helix	228-233	6
α-helix	235-236	2
β-strand	240-242	3	18
β-strand	248-250	3	18
α-helix	254-257	4
α-helix	259-262	4
α-helix	275-285	11
α-helix	291-296	6
β-strand	298-301	4	16
α-helix	303-305	3
β-strand	308	1	17
α-helix	310-321	12
α-helix	323	1
β-strand	328-331	4	16
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	9
α-helix	360-365	6
α-helix	368-375	8

Chain c: 2 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	13-15	3	14
α-helix	16-19	4
α-helix	41-42	2
β-strand	45-47	3	16

Chain C: 22 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	12-15	4	19
β-strand	20-23	4	19
β-strand	33-36	4	19
β-strand	40	1	20
β-strand	41-42	2	21
β-strand	45	1	22
β-strand	57	1	20
α-helix	60-64	5
β-strand	69-70	2	21
β-strand	75-76	2	23
β-strand	79-80	2	23
α-helix	83-94	12
β-strand	108-111	4	19
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-140	5	19
α-helix	142-150	9
β-strand	155-160	6	4
β-strand	165-170	6	4
β-strand	175	1	4
α-helix	177-179	3
β-strand	181-183	3	4
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	24
α-helix	228-233	6
α-helix	235-236	2
β-strand	240-242	3	25
β-strand	248-250	3	25
α-helix	254-257	4
α-helix	259-262	4
α-helix	275-285	11
α-helix	288-290	3
α-helix	291-296	6
β-strand	298-299	2	4
α-helix	304-306	3
β-strand	308	1	24
α-helix	310-321	12
α-helix	323	1
β-strand	330-331	2	4
β-strand	332	1	26
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	19
α-helix	360-365	6
α-helix	368-375	8

Chain d: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	13-15	3	30
α-helix	16-19	4

Chain D: 22 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	12-14	3	27
β-strand	15	1	28
β-strand	20-23	4	28
β-strand	25	1	27
β-strand	33-36	4	28
β-strand	39-42	4	29
β-strand	45	1	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	83-94	12
β-strand	108-111	4	27
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-140	5	27
α-helix	142-150	9
β-strand	155-160	6	14
β-strand	165-170	6	14
β-strand	175	1	14
α-helix	177-179	3
β-strand	183	1	14
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	32
α-helix	228-233	6
α-helix	235-236	2
β-strand	240-242	3	33
β-strand	248-250	3	33
α-helix	254-257	4
α-helix	259-262	4
α-helix	275-285	11
α-helix	288-290	3
α-helix	291-296	6
β-strand	298-301	4	14
α-helix	303-305	3
β-strand	308	1	32
α-helix	310-321	12
α-helix	323	1
β-strand	329-331	3	14
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	27
α-helix	360-365	6
α-helix	368-375	8

18 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
Actin related protein 1	A, B, C, D, E, F, G, I	protein	370	SUS SCROFA	F2Z5G5 (AlphaFold model)
Actin, cytoplasmic 1	H	protein	370	SUS SCROFA	Q6QAQ1 (AlphaFold model)
Actin related protein 11	J	protein	417	SUS SCROFA	I3LHK5 (AlphaFold model)
Capping protein (actin filament) muscle Z-line, alpha 1	K	protein	275	SUS SCROFA	A0PFK5 (AlphaFold model)
F-actin capping protein beta subunit variant II	L	protein	270	SUS SCROFA	D2JYW4
Dynactin subunit 2	M	protein	824	SUS SCROFA
Dynactin subunit 2	N	protein	818	SUS SCROFA
Dynactin subunit 3	O, P	protein	88	SUS SCROFA
Dynactin subunit 2	Q, R	protein	91	SUS SCROFA
Dynactin 5	U	protein	190	SUS SCROFA	D0G6S1
Dynactin subunit 6	V	protein	165	SUS SCROFA	A0A286ZK88
Dynactin subunit 2	Y	protein	243	SUS SCROFA

5 more molecules are not listed.

Sequence of entity 1 (A, B, C, D, E, F, G, I), FASTA

>5ADX_1 ACTIN RELATED PROTEIN 1 (chains A, B, C, D, E, F, G, I)
IANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHVRVMAGALEGDIFIGPKAEEHR
GLLSIRYPMEHGIVKDWNDMERIWQYVYSKEQLQTFSEEHPVLLTEAPLNPRKNRERAAE
VFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRIDIA
GRDVSRFLRLYLRKEGYDFHSSSEFEIVKAIKERACYLSINPQKDETLETEKAQYYLPDG
STIEIGPSRFRAPELLFRPDLIGEESEGIHEVLVFAIQKSDMDLRRTLFSNIVLSGGSTL
FKGFGDRLLSEVKKLAPKDVKIRISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEED
GARSIHRKTF

Sequence of entity 2 (H), FASTA

>5ADX_2 ACTIN, CYTOPLASMIC 1 (chains H)
AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGIL
TLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFE
TFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDL
TDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG
QVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTM
YPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDES
GPSIVHRKCF

Sequence of entity 3 (J), FASTA

>5ADX_3 ACTIN RELATED PROTEIN 11 (chains J)
MPLYEGLGSGGEKTAVVIDLGEAFTKCGFAGETGPRCIIPSVIKKAGMPKPIKVVQYNIN
TEELYSYLKEFIHILYFRHLLVNPRDRRVVVIESVLCPSHFRETLTRVLFKYFEVPSVLL
APSHLMALLTLGINSAMVLDCGYRESLVLPIYEGIPVLNCWGALPLGGKALHKELETQLL
EQCTVDTGAAKEQSLPSVMGSIPEGVLEDIKVRTCFVSDLTRGLKIQAAKFNIDGNTERP
SPPPNVDYPLDGEKILHVLGSIRDSVVEILFEQDNEEKSVATLILDSLMQCPIDTRKQLA
ENLVIIGGTSMLPGFLHRLLAEIRYLVEKPKYKKTLGTKTFRIHTPPAKANCVAWLGGAI
FGALQDILGSRSVSKEYYNQTGRIPDWCSLNNPPLEMVFDVGKSQPPLMKRAFSTEK

Sequence of entity 4 (K), FASTA

>5ADX_4 CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 (chains K)
RVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVK
IEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEVDGSLKSWRESCDS
ALRAYVKDHYSNGFCTVYAKNIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTA
QVVGVLKIQVHYYEDGNVQLVSHKDVQDSVTVSNEAQTAKEFIKIIEHAENEYQTAISEN
YQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGK

Sequence of entity 5 (L), FASTA

>5ADX_5 F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II (chains L)
SDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLL
CDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYL
WDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNK
SGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVN
GLRSVDVIPDNPKFQQLQRELSQVLTQRQI

Sequence of entity 6 (M), FASTA

>5ADX_6 DYNACTIN SUBUNIT 2 (chains M)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Sequence of entity 7 (N), FASTA

>5ADX_7 DYNACTIN SUBUNIT 2 (chains N)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Sequence of entity 8 (O, P), FASTA

>5ADX_8 DYNACTIN SUBUNIT 3 (chains O, P)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXX

Sequence of entity 9 (Q, R), FASTA

>5ADX_9 DYNACTIN SUBUNIT 2 (chains Q, R)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Sequence of entity 10 (U), FASTA

>5ADX_10 DYNACTIN 5 (chains U)
MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQA
LIINAHPDNITPDAEDSEPKPMIIGTNNVFEVGCYSQAMKMGDNNVIESKAYVGRNVILT
SGCIIGACCNLNTFEVIPENTVIYGADCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKT
MKGSSTPVKN

Sequence of entity 11 (V), FASTA

>5ADX_11 DYNACTIN SUBUNIT 6 (chains V)
SGNKVSRQSVLCGSQNIVLNGKTIVMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFS
KGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPE
TVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSYYQKFLPLTQV

Sequence of entity 12 (Y), FASTA

>5ADX_12 DYNACTIN SUBUNIT 2 (chains Y)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXX

Primary citation

The Structure of the Dynactin Complex and its Interaction with Dynein. Urnavicius, L., Zhang, K., Diamant, A.G. et al. Science (2015) 347:1441. DOI 10.1126/SCIENCE.AAA4080 · 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,…
6F1U 3.4 Å, N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1
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
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

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