9E0X: Phi dynein

Cryo-EM structure of Phi dynein. Determined by electron microscopy at 2.7 Å resolution. Released 9 Jul 2025.

Method: Electron microscopy
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 2
Atoms: 46,234
Mol. weight: 1111.93 kDa
Ligands: MG, ATP, ADP
Released: 9 Jul 2025

Explore 9E0X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9E0X contains 279 α-helices and 140 β-strands across 2 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: 139 helices, 72 β-strands

Element	Residues	Length	Sheet
α-helix	1445-1472	28
β-strand	1474	1	1
β-strand	1476-1480	5	2
β-strand	1484-1488	5	2
α-helix	1490-1509	20
α-helix	1517-1553	37
α-helix	1557-1560	4
α-helix	1562-1584	23
β-strand	1587	1	1
α-helix	1588-1592	5
α-helix	1597-1613	17
α-helix	1616-1625	10
α-helix	1627-1631	5
α-helix	1634-1642	9
α-helix	1649-1653	5
α-helix	1654-1657	4
β-strand	1663-1666	4	3
β-strand	1672-1677	6	3
β-strand	1683-1691	9	3
α-helix	1698-1728	31
α-helix	1735-1744	10
α-helix	1747-1767	21
α-helix	1776-1797	22
α-helix	1802-1827	26
α-helix	1836-1839	4
β-strand	1843-1846	4	4
β-strand	1857-1861	5	4
β-strand	1864-1867	4	4
α-helix	1878-1880	3
α-helix	1883-1897	15
β-strand	1901-1905	5	5
α-helix	1913-1923	11
β-strand	1927-1931	5	5
α-helix	1938-1951	14
β-strand	1954-1958	5	5
α-helix	1960-1962	3
α-helix	1965-1986	22
β-strand	1998-2001	4	6
β-strand	2004-2007	4	6
β-strand	2013-2018	6	5
α-helix	2026-2029	4
α-helix	2030-2033	4
β-strand	2036-2040	5	5
α-helix	2046-2057	12
α-helix	2062-2079	18
α-helix	2090-2113	24
α-helix	2133-2145	13
α-helix	2146-2148	3
α-helix	2154-2164	11
α-helix	2176-2188	13
α-helix	2201-2216	16
β-strand	2219-2223	5	7
α-helix	2230-2245	16
α-helix	2247-2248	2
β-strand	2249-2254	6	7
α-helix	2261-2265	5
β-strand	2266-2268	3	8
β-strand	2275-2277	3	8
α-helix	2279-2289	11
α-helix	2294-2296	3
β-strand	2298-2304	7	7
α-helix	2316-2319	4
β-strand	2324-2326	3	9
β-strand	2332-2334	3	9
β-strand	2339-2345	7	7
α-helix	2353-2358	6
β-strand	2360-2363	4	7
α-helix	2371-2383	13
α-helix	2411-2423	13
α-helix	2424-2426	3
α-helix	2433-2440	8
α-helix	2448-2449	2
α-helix	2451-2475	25
α-helix	2483-2503	21
α-helix	2508-2521	14
α-helix	2534-2536	3
β-strand	2537-2539	3	10
β-strand	2545-2547	3	10
α-helix	2572-2586	15
β-strand	2591-2594	4	11
α-helix	2601-2610	10
β-strand	2615-2620	6	11
α-helix	2628-2638	11
β-strand	2639-2643	5	12
β-strand	2648-2652	5	12
β-strand	2658-2663	6	11
α-helix	2670-2671	2
α-helix	2678-2688	11
β-strand	2691-2694	4	12
β-strand	2699-2703	5	12
β-strand	2706-2712	7	11
α-helix	2722-2724	3
α-helix	2725-2730	6
β-strand	2733-2735	3	11
α-helix	2741-2755	15
α-helix	2767-2783	17
α-helix	2796-2810	15
α-helix	2818-2833	16
α-helix	2840-2857	18
α-helix	2863-2866	4
β-strand	2872-2874	3	13
β-strand	2882-2884	3	13
α-helix	2886-2903	18
α-helix	2913-2927	15
β-strand	2932-2937	6	14
α-helix	2944-2954	11
α-helix	2956	1
β-strand	2957-2959	3	14
α-helix	2969-2984	16
β-strand	2990-2995	6	14
α-helix	3002-3014	13
α-helix	3024-3040	17
α-helix	3048-3061	14
β-strand	3062-3068	7	14
α-helix	3072-3081	10
α-helix	3084-3087	4
β-strand	3089-3095	7	14
α-helix	3097-3098	2
α-helix	3099-3110	12
α-helix	3139-3164	26
α-helix	3173-3252	80
α-helix	3436-3499	64
α-helix	3503-3516	14
α-helix	3522-3538	17
α-helix	3549-3553	5
α-helix	3556-3564	9
α-helix	3571-3582	12
α-helix	3586	1
β-strand	3587-3590	4	15
α-helix	3595-3603	9
α-helix	3609	1
β-strand	3610-3613	4	15
α-helix	3617-3619	3
α-helix	3620-3629	10
β-strand	3633-3636	4	15
α-helix	3638-3640	3
α-helix	3643-3645	3
α-helix	3646-3650	5
β-strand	3654	1	16
β-strand	3661-3664	4	16
β-strand	3667-3670	4	16
β-strand	3677-3681	5	15
α-helix	3690-3695	6
β-strand	3697-3700	4	15
α-helix	3705-3720	16
α-helix	3722-3755	34
α-helix	3764-3817	54
α-helix	3818-3820	3
α-helix	3829-3836	8
α-helix	3837-3841	5
α-helix	3854-3873	20
α-helix	3877-3894	18
α-helix	3902-3909	8
α-helix	3911-3913	3
α-helix	3929-3938	10
α-helix	3948-3953	6
α-helix	3982-3996	15
α-helix	3998-4000	3
α-helix	4001-4012	12
α-helix	4020-4022	3
α-helix	4024-4025	2
α-helix	4027-4029	3
α-helix	4030-4034	5
β-strand	4041-4045	5	17
α-helix	4052-4062	11
β-strand	4068-4070	3	17
α-helix	4074-4090	17
β-strand	4094-4097	4	17
α-helix	4099-4101	3
α-helix	4103-4115	13
β-strand	4124-4129	6	17
α-helix	4136-4141	6
β-strand	4143-4147	5	17
α-helix	4153-4163	11
α-helix	4166-4169	4
α-helix	4175-4195	21
α-helix	4209-4226	18
α-helix	4240-4246	7
α-helix	4247-4251	5
α-helix	4259-4273	15
β-strand	4283-4285	3	18
β-strand	4294-4295	2	18
α-helix	4296-4297	2
α-helix	4302-4311	10
α-helix	4318-4321	4
α-helix	4327-4349	23
α-helix	4380-4390	11
α-helix	4392-4394	3
α-helix	4408-4438	31
α-helix	4443-4445	3
α-helix	4446-4457	12
β-strand	4459	1	19
α-helix	4460-4461	2
β-strand	4474	1	19
α-helix	4475-4497	23
α-helix	4503-4506	4
β-strand	4509-4510	2	20
α-helix	4511-4513	3
α-helix	4517-4532	16
β-strand	4540-4544	5	20
β-strand	4558-4561	4	20
β-strand	4563-4564	2	21
β-strand	4568-4570	3	22
β-strand	4575-4577	3	22
β-strand	4584-4585	2	21
β-strand	4588-4593	6	20
β-strand	4605-4610	6	21
β-strand	4618-4624	7	21
α-helix	4625-4627	3
α-helix	4632-4638	7
β-strand	4642-4643	2	21

Chain B: 140 helices, 68 β-strands

Element	Residues	Length	Sheet
α-helix	1445-1472	28
β-strand	1474	1	23
β-strand	1476-1480	5	24
β-strand	1484-1488	5	24
α-helix	1490-1509	20
α-helix	1517-1553	37
α-helix	1562-1584	23
β-strand	1587	1	23
α-helix	1588-1593	6
α-helix	1597-1613	17
α-helix	1616-1625	10
α-helix	1627-1631	5
α-helix	1634-1642	9
α-helix	1648-1653	6
α-helix	1654-1657	4
β-strand	1663-1666	4	25
β-strand	1672-1677	6	25
β-strand	1683-1691	9	25
α-helix	1698-1728	31
α-helix	1735-1744	10
α-helix	1747-1767	21
α-helix	1776-1797	22
α-helix	1802-1827	26
α-helix	1836-1839	4
β-strand	1843-1846	4	26
β-strand	1857-1861	5	26
β-strand	1864-1867	4	26
α-helix	1883-1897	15
β-strand	1901-1905	5	27
α-helix	1912-1923	12
β-strand	1927-1931	5	27
α-helix	1938-1951	14
β-strand	1954-1958	5	27
α-helix	1960-1962	3
α-helix	1965-1986	22
β-strand	1998-2001	4	28
β-strand	2004-2007	4	28
β-strand	2013-2018	6	27
α-helix	2025-2029	5
α-helix	2030-2033	4
β-strand	2036-2040	5	27
α-helix	2046-2057	12
α-helix	2062-2079	18
α-helix	2090-2113	24
α-helix	2133-2145	13
α-helix	2146-2148	3
α-helix	2151-2153	3
α-helix	2154-2164	11
α-helix	2176-2188	13
α-helix	2201-2216	16
β-strand	2219-2223	5	29
α-helix	2230-2245	16
α-helix	2247-2248	2
β-strand	2249-2254	6	29
α-helix	2261-2265	5
β-strand	2266-2268	3	30
β-strand	2275-2277	3	30
α-helix	2279-2289	11
α-helix	2294-2296	3
β-strand	2298-2304	7	29
α-helix	2316-2319	4
β-strand	2324-2326	3	31
β-strand	2332-2334	3	31
α-helix	2335-2336	2
β-strand	2339-2345	7	29
α-helix	2353-2358	6
β-strand	2360-2363	4	29
α-helix	2371-2383	13
α-helix	2411-2423	13
α-helix	2424-2426	3
α-helix	2433-2442	10
α-helix	2448-2449	2
α-helix	2451-2475	25
α-helix	2483-2503	21
α-helix	2508-2521	14
α-helix	2534-2536	3
β-strand	2537-2539	3	32
β-strand	2545-2547	3	32
α-helix	2548-2550	3
α-helix	2572-2586	15
β-strand	2591-2594	4	33
α-helix	2601-2610	10
β-strand	2615-2620	6	33
α-helix	2628-2638	11
β-strand	2639-2643	5	34
β-strand	2648-2652	5	34
β-strand	2658-2663	6	33
α-helix	2670-2671	2
α-helix	2678-2688	11
β-strand	2691-2694	4	34
β-strand	2699-2703	5	34
β-strand	2706-2712	7	33
α-helix	2722-2724	3
α-helix	2725-2728	4
β-strand	2733-2735	3	33
α-helix	2741-2755	15
α-helix	2760-2762	3
α-helix	2767-2783	17
α-helix	2796-2810	15
α-helix	2818-2833	16
α-helix	2840-2857	18
α-helix	2863-2866	4
β-strand	2873-2874	2	35
β-strand	2882-2883	2	35
α-helix	2886-2903	18
α-helix	2913-2927	15
β-strand	2932-2937	6	36
α-helix	2944-2954	11
α-helix	2956	1
β-strand	2957-2959	3	36
α-helix	2969-2980	12
α-helix	2981-2985	5
β-strand	2990-2995	6	36
α-helix	3002-3014	13
α-helix	3024-3040	17
α-helix	3048-3061	14
β-strand	3062-3068	7	36
α-helix	3072-3081	10
α-helix	3084-3087	4
β-strand	3089-3095	7	36
α-helix	3097-3098	2
α-helix	3099-3110	12
α-helix	3121-3123	3
α-helix	3139-3164	26
α-helix	3173-3252	80
α-helix	3436-3516	81
α-helix	3522-3538	17
α-helix	3549-3553	5
α-helix	3556-3564	9
α-helix	3571-3582	12
α-helix	3586	1
β-strand	3587-3590	4	37
α-helix	3595-3603	9
α-helix	3609	1
β-strand	3610-3613	4	37
α-helix	3617-3619	3
α-helix	3620-3629	10
β-strand	3633-3636	4	37
α-helix	3638-3640	3
α-helix	3643-3645	3
α-helix	3646-3650	5
β-strand	3654	1	38
β-strand	3661-3664	4	38
β-strand	3667-3670	4	38
α-helix	3671-3672	2
β-strand	3677-3681	5	37
α-helix	3687-3689	3
α-helix	3690-3695	6
β-strand	3697-3700	4	37
α-helix	3705-3720	16
α-helix	3722-3754	33
α-helix	3764-3817	54
α-helix	3819-3822	4
α-helix	3829-3836	8
α-helix	3837-3841	5
α-helix	3854-3873	20
α-helix	3877-3894	18
α-helix	3902-3909	8
α-helix	3910-3913	4
α-helix	3929-3938	10
α-helix	3948-3953	6
α-helix	3982-3996	15
α-helix	3998-4000	3
α-helix	4001-4012	12
α-helix	4024-4025	2
α-helix	4027-4029	3
α-helix	4030-4034	5
β-strand	4041-4045	5	39
α-helix	4052-4062	11
β-strand	4066-4070	5	39
α-helix	4074-4090	17
β-strand	4093-4097	5	39
α-helix	4099-4101	3
α-helix	4103-4115	13
β-strand	4124-4129	6	39
α-helix	4136-4141	6
β-strand	4143-4147	5	39
α-helix	4153-4163	11
α-helix	4166-4169	4
α-helix	4175-4195	21
α-helix	4209-4226	18
α-helix	4235-4237	3
α-helix	4240-4246	7
α-helix	4247-4251	5
α-helix	4259-4272	14
β-strand	4285	1	40
β-strand	4294	1	40
α-helix	4302-4311	10
α-helix	4318-4321	4
α-helix	4327-4349	23
α-helix	4380-4390	11
α-helix	4391-4394	4
α-helix	4408-4438	31
α-helix	4446-4457	12
α-helix	4459-4461	3
α-helix	4475-4497	23
α-helix	4503-4505	3
β-strand	4509-4510	2	41
α-helix	4517-4532	16
β-strand	4542-4544	3	41
β-strand	4558-4561	4	41
β-strand	4563-4570	8	42
β-strand	4575-4585	11	42
β-strand	4588-4591	4	41
β-strand	4605-4610	6	42
β-strand	4618-4624	7	42
α-helix	4632-4638	7
β-strand	4641-4643	3	42

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytoplasmic dynein 1 heavy chain 1	A, B	protein	4843	Homo sapiens	Q14204

Sequence of entity 1 (A, B), FASTA

>9E0X_1 Cytoplasmic dynein 1 heavy chain 1 (chains A, B)
GDYDIPTTENLYFQGDKDCEMKRTTLDSPLGKLELSGCEQGLHRIIFLGKGTSAADAVEV
PAPAAVLGGPEPLMQATAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVV
KFGEVISYSHLAALAGNPAATAAVKTALSGNPVPILIPCHRVVQGDLDVGGYEGGLAVKE
WLLAHEGHRLGKPGLGGSSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLE
DGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVERSTLKEDVGDEGEEEKEFISYNI
NIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPFFKS
YIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYER
GEKPKVTDFGDKVEDPTFLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLER
ALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDTGLKQALETVNDYNPLMKDFPLND
LLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRKLMH
VAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARL
DQMRKFRRQHEQLRAVIVRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEV
NLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRVETRITARLRDQLGTAKNANEMFR
IFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRDLPP
VSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWA
RKVQQRNLGVSGRIFTIESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLA
IVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNTISLLVAGLKKEVQALIAEGIALV
WESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNRVQK
AVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAP
QVSHKPGGEPKIKNVVHELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQR
YQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAVMGIVSEVEQYVKVWLQYQCLWDM
QAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKYDSW
HKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQF
EKQVELYRNGQRLLEKQRFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKI
VQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQALTIYEGKFGRLKDDREKCAKAKEA
LELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLRQNL
DALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVN
WVVSELTLGQIWDVDLQKNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNK
CRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDALSWEDKLNRIMALFDVWIDVQRR
WVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRSLER
LADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSS
IILNEDNSVVLGISSREGEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTE
VEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSENVETALSSMGGGGDAAPLHSVLS
NVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLSQMR
FYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGS
PFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRL
EERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCELLNKQVKVSPDMAIFITMNPGYA
GRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQLSSQ
SHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCE
TMVPKLVAEDIPLLFSLLSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMW
VEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKALERLEGVEGVAHIIDPKAISKDH
LYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLDDNK
LLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLR
SIPLDEGEDEAQRRRKGKEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQL
EHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFPMQIEQLERYIQRYLVYAILWSLS
GDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETHKVA
APDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFS
SATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFI
RQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVDYPGPAS
LTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMTRWV
RGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDR
EKAMSRPILYSNWLSKDYIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRID
RIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRS
GCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLM
LDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALY
QVGKEFTSKMDLEKPNYIVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAK
RGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLR
IKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLD
KVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIM
RENFIPTIVNFSAEEISDAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYA
DMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKA
DLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQ
MRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRF
NRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDP
VLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTV
TRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDD
DTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHF
LYQYSLQFFLDIYHNVLYENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITF
AMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGSTPRIQGLTVEQAEAVVRLSCLPA
FKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDRLLA
MAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQN
TQITSIAIGSAEGFNQADKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFR
LFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRTFSSIPVSRICKSPNERARLYFLL
AWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPWSAL
KTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRRE
EFVQWVELLPDTQTPSWLGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKK
TRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKRTVENIKDPLFRFFEREVKMGAKL
LQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFS
ERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEV
NVTTSQGATLDACSFGVTGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKAS
VVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGVAVLCTE

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	4
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6

Primary citation

Cryo-EM captures early intermediate steps in dynein activation by LIS1. Nguyen, K.H.V., Karasmanis, E.P., Kendrick, A.A. et al. Nat Commun (2025) 16:7054-7054. DOI 10.1038/s41467-025-62185-z · PubMed

Other PDB entries of the same protein (UniProt Q14204), best resolution first:

5OWO 1.79 Å, Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution
9BLZ 2.2 Å, State-1(phi motor) of full-length human dynein-1 in 5mM ATP
9BMR 2.6 Å, State-1 of motor domain from full-length human phi dynein-1 in 5 mM ADP
9DH5 2.6 Å, State-1 of the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+
9E10 2.71 Å, Dimeric motor domains from phi dynein-1 under Lis1 condition
9BM0 2.8 Å, State-2 of motor domain from full-length human dynein-1 in 5mM ATP
9BMF 2.8 Å, State-1(phi motor) of full-length human dynein-1 in 5mM ATPVi
9BMH 2.8 Å, State-4 of motor domain from full-length human dynein-1 in 5mM ATPVi
9BN3 2.8 Å, The alpha registry-locked dynein motor domain mutant in 5mM ATP condition, class1
9BM2 2.82 Å, State-4 of motor domain from full-length human dynein-1 in 5 mM ATP
9BMG 2.86 Å, State-2 of full-length human dynein-1 in 5mM ATPVi
9BMY 2.86 Å, State-1 of motor domain from full-length human dynein-1 in apo condition

Browse structure collections

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