9B85: Human dynactin complex

Cryo-EM structure of human dynactin complex bound to Chlamydia effector Dre1. Determined by electron microscopy at 3.47 Å resolution. Released 16 Apr 2025.

Method: Electron microscopy
Resolution: 3.47 Å
Organism: Homo sapiens
Chains: 19
Atoms: 41,244
Mol. weight: 767.74 kDa
Ligands: ADP, ANP, ZN
Released: 16 Apr 2025

Explore 9B85 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9B85 contains 290 α-helices and 325 β-strands across 19 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: 25 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	10-11	2
β-strand	12-15	4	1
β-strand	20-25	6	1
β-strand	33-36	4	1
β-strand	39-42	4	2
α-helix	45	1
β-strand	46	1	3
α-helix	51-53	3
β-strand	57	1	2
α-helix	60-64	5
α-helix	66-68	3
β-strand	69-72	4	2
β-strand	75-76	2	4
β-strand	79-80	2	4
α-helix	83-94	12
β-strand	108-112	5	1
α-helix	113	1
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-141	6	1
α-helix	142-150	9
β-strand	155-160	6	5
β-strand	165-171	7	5
β-strand	174-175	2	5
β-strand	181-183	3	5
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	6
α-helix	228-233	6
α-helix	235-237	3
β-strand	240-242	3	7
β-strand	248-250	3	7
α-helix	254-257	4
α-helix	259-262	4
α-helix	275-284	10
α-helix	288-296	9
β-strand	298-301	4	5
α-helix	303-305	3
β-strand	308	1	6
α-helix	310-321	12
α-helix	323	1
β-strand	330-331	2	5
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	1
α-helix	360-366	7
α-helix	369-374	6

Chain B: 23 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	2013	1
β-strand	2014-2017	4	8
β-strand	2022-2027	6	8
β-strand	2035-2038	4	8
β-strand	2041-2044	4	9
β-strand	2047-2048	2	10
β-strand	2059	1	9
α-helix	2062-2066	5
α-helix	2068-2070	3
β-strand	2071-2074	4	9
β-strand	2077-2078	2	11
β-strand	2081-2082	2	11
α-helix	2085-2095	11
β-strand	2110-2114	5	8
α-helix	2115	1
α-helix	2120-2132	13
β-strand	2138-2143	6	8
α-helix	2144-2152	9
β-strand	2157-2162	6	12
β-strand	2167-2173	7	12
β-strand	2176-2177	2	12
β-strand	2183-2185	3	12
α-helix	2189-2203	15
α-helix	2210-2222	13
β-strand	2225	1	13
α-helix	2230-2235	6
α-helix	2237-2238	2
β-strand	2242-2244	3	14
β-strand	2250-2252	3	14
α-helix	2256-2259	4
α-helix	2261-2264	4
α-helix	2267-2269	3
α-helix	2277-2287	11
α-helix	2290-2298	9
β-strand	2300-2303	4	12
α-helix	2305-2308	4
β-strand	2310	1	13
α-helix	2312-2323	12
α-helix	2325	1
β-strand	2330-2333	4	12
α-helix	2341-2351	11
α-helix	2355-2358	4
β-strand	2360-2361	2	8
α-helix	2362-2368	7
α-helix	2370-2375	6

Chain C: 22 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	10-11	2
β-strand	12-15	4	15
β-strand	20-25	6	15
β-strand	33-36	4	15
β-strand	39-42	4	16
β-strand	45-46	2	17
β-strand	57	1	16
α-helix	60-64	5
α-helix	66-68	3
β-strand	69-72	4	16
β-strand	75-76	2	18
β-strand	79-80	2	18
α-helix	83-93	11
β-strand	108-112	5	15
α-helix	113	1
α-helix	118-130	13
β-strand	136-141	6	15
α-helix	142-150	9
β-strand	155-160	6	3
β-strand	165-171	7	3
β-strand	174-175	2	3
β-strand	181-183	3	3
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	19
α-helix	228-233	6
β-strand	240-242	3	20
β-strand	248-250	3	20
α-helix	254-257	4
α-helix	259-262	4
α-helix	265-267	3
α-helix	275-284	10
α-helix	288-296	9
β-strand	298-301	4	3
α-helix	303-305	3
β-strand	308	1	19
α-helix	310-321	12
α-helix	323	1
β-strand	330-333	4	3
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	15
α-helix	360-366	7
α-helix	368-372	5

Chain D: 22 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	10-11	2
β-strand	12-15	4	21
β-strand	20-25	6	21
β-strand	33-36	4	21
β-strand	39-42	4	22
β-strand	45-46	2	23
β-strand	57	1	22
α-helix	60-64	5
α-helix	66-68	3
β-strand	69-72	4	22
β-strand	75-76	2	24
β-strand	79-80	2	24
α-helix	83-93	11
β-strand	108-112	5	21
α-helix	113	1
α-helix	118-130	13
β-strand	136-141	6	21
α-helix	142-150	9
β-strand	155-160	6	10
β-strand	165-171	7	10
β-strand	174-175	2	10
β-strand	181-183	3	10
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	25
α-helix	228-234	7
β-strand	240-242	3	26
β-strand	248-250	3	26
α-helix	254-257	4
α-helix	259-262	4
α-helix	265-267	3
α-helix	275-284	10
α-helix	288-296	9
β-strand	298-301	4	10
α-helix	303-305	3
β-strand	308	1	25
α-helix	310-321	12
α-helix	323	1
β-strand	329-331	3	10
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	21
α-helix	360-366	7
α-helix	368-373	6

Chain E: 22 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	9-11	3
β-strand	12-15	4	27
β-strand	20-25	6	27
β-strand	33-36	4	27
β-strand	39-42	4	28
β-strand	45-46	2	29
β-strand	57-58	2	28
α-helix	60-64	5
β-strand	69-72	4	28
β-strand	75-76	2	30
β-strand	79-80	2	30
α-helix	83-93	11
β-strand	108-112	5	27
α-helix	113	1
α-helix	118-130	13
β-strand	136-141	6	27
α-helix	142-150	9
β-strand	155-160	6	17
β-strand	165-171	7	17
β-strand	174-175	2	17
β-strand	181-183	3	17
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	31
α-helix	228-233	6
α-helix	235-236	2
β-strand	240-242	3	32
β-strand	248-250	3	32
α-helix	254-257	4
α-helix	259-262	4
α-helix	265-267	3
α-helix	275-284	10
α-helix	288-296	9
β-strand	298-301	4	17
α-helix	303-305	3
β-strand	308	1	31
α-helix	310-321	12
α-helix	323	1
β-strand	329-331	3	17
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	27
α-helix	360-366	7
α-helix	368-373	6

Chain F: 23 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	9-11	3
β-strand	12-15	4	33
β-strand	20-25	6	33
β-strand	33-36	4	33
β-strand	39-42	4	34
β-strand	45-46	2	35
α-helix	52-53	2
β-strand	57	1	34
α-helix	60-64	5
β-strand	69-72	4	34
β-strand	75-76	2	36
β-strand	79-80	2	36
α-helix	83-94	12
β-strand	108-112	5	33
α-helix	113	1
α-helix	118-126	9
α-helix	127-131	5
β-strand	136-141	6	33
α-helix	142-150	9
β-strand	155-160	6	23
β-strand	165-171	7	23
β-strand	174-175	2	23
β-strand	181-183	3	23
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	37
α-helix	228-233	6
α-helix	235-237	3
β-strand	240-242	3	38
β-strand	248-250	3	38
α-helix	254-257	4
α-helix	259-262	4
α-helix	275-285	11
α-helix	288-296	9
β-strand	298-301	4	23
α-helix	303-305	3
β-strand	308	1	37
α-helix	310-321	12
α-helix	323	1
β-strand	329-331	3	23
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	33
α-helix	360-366	7
α-helix	369-374	6

Chain G: 24 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	10-11	2
β-strand	12-15	4	39
β-strand	20-25	6	39
β-strand	33-36	4	39
β-strand	39-42	4	40
α-helix	45-46	2
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	41
β-strand	79-80	2	41
α-helix	83-94	12
β-strand	108-112	5	39
α-helix	113	1
α-helix	118-130	13
β-strand	136-141	6	39
α-helix	142-150	9
β-strand	155-160	6	29
β-strand	165-171	7	29
β-strand	174-175	2	29
α-helix	177-179	3
β-strand	181-183	3	29
α-helix	187-201	15
α-helix	208-220	13
β-strand	223	1	42
α-helix	228-233	6
α-helix	235-237	3
β-strand	240-242	3	43
β-strand	248-250	3	43
α-helix	254-257	4
α-helix	259-262	4
α-helix	275-284	10
α-helix	291-296	6
β-strand	298-301	4	29
α-helix	303-305	3
β-strand	308	1	42
α-helix	310-321	12
α-helix	323	1
β-strand	330-333	4	29
α-helix	339-349	11
α-helix	353-356	4
β-strand	358-359	2	39
α-helix	360-366	7
α-helix	369-374	6

Chain H: 20 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	44
β-strand	16-21	6	44
β-strand	29-32	4	44
β-strand	35-38	4	45
β-strand	53-54	2	45
α-helix	56-60	5
β-strand	65-68	4	45
β-strand	71-72	2	46
β-strand	75-76	2	46
α-helix	79-87	9
α-helix	88-94	7
β-strand	103-107	5	44
α-helix	113-125	13
β-strand	131-136	6	44
α-helix	137-145	9
β-strand	150-155	6	35
β-strand	160-166	7	35
β-strand	169-170	2	35
α-helix	172-174	3
β-strand	176-178	3	35
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	239-241	3	47
β-strand	247-249	3	47
α-helix	251-254	4
α-helix	257-261	5
α-helix	264-266	3
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	35
α-helix	309-320	12
β-strand	329-330	2	35
α-helix	338-348	11
α-helix	350-354	5
α-helix	356	1
β-strand	357-358	2	44
α-helix	359-365	7
α-helix	369-372	4

11 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
Alpha-centractin	A, B, C, D, E, F, G, I	protein	376	Homo sapiens	P61163 (AlphaFold model)
Actin, cytoplasmic 1	H	protein	375	Homo sapiens	P60709 (AlphaFold model)
Actin-related protein 10	J	protein	417	Homo sapiens	Q9NZ32 (AlphaFold model)
Dynactin subunit 4	K	protein	460	Homo sapiens	Q9UJW0 (AlphaFold model)
Dynactin subunit 5	L	protein	182	Homo sapiens	Q9BTE1
Dynactin subunit 6	M	protein	190	Homo sapiens	O00399
F-actin-capping protein subunit alpha-1	N	protein	286	Homo sapiens	P52907
F-actin-capping protein subunit beta	O	protein	272	Homo sapiens	P47756
Dynactin subunit 2	P, Q, p, q	protein	401	Homo sapiens	Q13561

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

>9B85_1 Alpha-centractin (chains A, B, C, D, E, F, G, I)
MESYDVIANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHVRVMAGALEGDIFIGP
KAEEHRGLLSIRYPMEHGIVKDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPRKN
RERAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSI
MRIDIAGRDVSRFLRLYLRKEGYDFHSSSEFEIVKAIKERACYLSINPQKDETLETEKAQ
YYLPDGSTIEIGPSRFRAPELLFRPDLIGEESEGIHEVLVFAIQKSDMDLRRTLFSNIVL
SGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPQERLYSTWIGGSILASLDTFKKMWVSK
KEYEEDGARSIHRKTF

Sequence of entity 2 (H), FASTA

>9B85_2 Actin, cytoplasmic 1 (chains H)
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT
QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL
AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ
EYDESGPSIVHRKCF

Sequence of entity 3 (J), FASTA

>9B85_3 Actin-related protein 10 (chains J)
MPLYEGLGSGGEKTAVVIDLGEAFTKCGFAGETGPRCIIPSVIKRAGMPKPVRVVQYNIN
TEELYSYLKEFIHILYFRHLLVNPRDRRVVIIESVLCPSHFRETLTRVLFKYFEVPSVLL
APSHLMALLTLGINSAMVLDCGYRESLVLPIYEGIPVLNCWGALPLGGKALHKELETQLL
EQCTVDTSVAKEQSLPSVMGSVPEGVLEDIKARTCFVSDLKRGLKIQAAKFNIDGNNERP
SPPPNVDYPLDGEKILHILGSIRDSVVEILFEQDNEEQSVATLILDSLIQCPIDTRKQLA
ENLVVIGGTSMLPGFLHRLLAEIRYLVEKPKYKKALGTKTFRIHTPPAKANCVAWLGGAI
FGALQDILGSRSVSKEYYNQTGRIPDWCSLNNPPLEMMFDVGKTQPPLMKRAFSTEK

Sequence of entity 4 (K), FASTA

>9B85_4 Dynactin subunit 4 (chains K)
MASLLQSDRVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPS
AEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRD
VGMADKSVASGGWQEPENPHTQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSD
KYGLGTRLQRPRAGASISTLAGLSLKEGEDQKEIKIEPAQAVDEVEPLPEDYYTRPVNLT
EVTTLQQRLLQPDFQPVCASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQL
VAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLFECEEGDPDDINSTAKVVV
PPKELVLAGKDAAAEYDELAEPQDFQDDPDIIAFRKANKVGIFIKVTPQREEGEVTVCFK
MKHDFKNLAAPIRPIEESDQGTEVIWLTQHVELSLGPLLP

Sequence of entity 5 (L), FASTA

>9B85_5 Dynactin subunit 5 (chains L)
MELGELLYNKSEYIETASGNKVSRQSVLCGSQNIVLNGKTIVMNDCIIRGDLANVRVGRH
CVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRC
VLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSYYQKFLPLT
QV

Sequence of entity 6 (M), FASTA

>9B85_6 Dynactin subunit 6 (chains M)
MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQA
LIINAYPDNITPDTEDPEPKPMIIGTNNVFEVGCYSQAMKMGDNNVIESKAYVGRNVILT
SGCIIGACCNLNTFEVIPENTVIYGADCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKT
MKGSSTPVKN

Sequence of entity 7 (N), FASTA

>9B85_7 F-actin-capping protein subunit alpha-1 (chains N)
MADFDDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEADGGLKSW
RESCDSALRAYVKDHYSNGFCTVYAKTIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSLTVSNEAQTAKEFIKIIENAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA

Sequence of entity 8 (O), FASTA

>9B85_8 F-actin-capping protein subunit beta (chains O)
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN
KSGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV
NGLRSVQTFADKSKQEALKNDLVEALKRKQQC

Sequence of entity 9 (P, Q, p, q), FASTA

>9B85_9 Dynactin subunit 2 (chains P, Q, p, q)
MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELTSTSVEHIIVNPNAAYDKFKDK
RVGTKGLDFSDRIGKTKRTGYESGEYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKI
KTTVKESATEEKLTPVLLAKQLAALKQQLVASHLEKLLGPDAAINLTDPDGALAKRLLLQ
LEATKNSKGGSGGKTTGTPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELETAVRC
DQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASV
EDADTQSKVHQLYETIQRWSPIASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMI
ANSLKDNTTLLTQVQTTMRENLATVEGNFASIDERMKKLGK

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	8
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	1
ZN	Zinc ion	Zn	3

Primary citation

The Chlamydia effector Dre1 binds dynactin to reposition host organelles during infection. Sherry, J., Pawar, K.I., Dolat, L. et al. Cell Rep (2025) 44:115509-115509. DOI 10.1016/j.celrep.2025.115509 · PubMed

Other PDB entries of the same protein (UniProt P61163 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9B7J 3.49 Å, Cryo-EM structure of human dynactin complex bound to Chlamydia effector Dre1

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