9E11: Dimeric motor domains from phi-like dynein-1

Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dimer under Lis1 condition. Determined by electron microscopy at 2.86 Å resolution. Released 6 Aug 2025.

Method: Electron microscopy
Resolution: 2.86 Å
Organism: Homo sapiens
Chains: 4
Atoms: 52,502
Mol. weight: 1163.26 kDa
Ligands: MG, ATP, ADP
Released: 6 Aug 2025

Explore 9E11 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9E11 contains 329 α-helices and 192 β-strands across 4 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: 160 helices, 68 β-strands

Element	Residues	Length	Sheet
α-helix	1462-1471	10
β-strand	1474	1	1
β-strand	1478-1480	3	2
β-strand	1484-1486	3	2
α-helix	1491-1509	19
α-helix	1511-1513	3
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	1597-1612	16
α-helix	1616-1622	7
α-helix	1627-1631	5
α-helix	1634-1642	9
α-helix	1647-1650	4
β-strand	1663-1666	4	3
β-strand	1672-1677	6	3
β-strand	1683-1691	9	3
α-helix	1698-1724	27
α-helix	1735-1744	10
α-helix	1747-1768	22
α-helix	1769-1771	3
α-helix	1778-1796	19
α-helix	1802-1828	27
α-helix	1836-1839	4
β-strand	1842-1846	5	4
α-helix	1853-1855	3
β-strand	1857-1861	5	4
β-strand	1864-1867	4	4
α-helix	1877-1880	4
α-helix	1883-1897	15
β-strand	1901-1905	5	5
α-helix	1913-1922	10
β-strand	1927-1931	5	5
α-helix	1938-1951	14
β-strand	1954-1958	5	5
α-helix	1960-1962	3
α-helix	1965-1985	21
α-helix	1995-1997	3
β-strand	1998-2001	4	6
β-strand	2004-2007	4	6
β-strand	2013-2018	6	5
α-helix	2025-2029	5
α-helix	2030-2033	4
β-strand	2036-2040	5	5
α-helix	2046-2055	10
α-helix	2062-2079	18
α-helix	2081-2082	2
α-helix	2090-2116	27
α-helix	2124-2129	6
α-helix	2133-2145	13
α-helix	2146-2148	3
α-helix	2153-2164	12
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	2309-2312	4
α-helix	2313-2315	3
β-strand	2324-2326	3	9
β-strand	2332-2334	3	9
α-helix	2335-2336	2
β-strand	2339-2345	7	7
α-helix	2353-2357	5
β-strand	2360-2363	4	7
α-helix	2366-2368	3
α-helix	2371-2384	14
α-helix	2411-2423	13
α-helix	2432-2440	9
α-helix	2451-2475	25
α-helix	2483-2502	20
α-helix	2508-2521	14
α-helix	2534-2536	3
β-strand	2537-2539	3	10
β-strand	2545-2547	3	10
α-helix	2548-2551	4
α-helix	2559-2561	3
α-helix	2572-2585	14
β-strand	2591-2594	4	11
α-helix	2601-2609	9
β-strand	2615-2620	6	11
α-helix	2628-2638	11
β-strand	2639-2644	6	12
β-strand	2647-2652	6	12
β-strand	2658-2663	6	11
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	2725-2728	4
β-strand	2733-2735	3	11
α-helix	2737-2739	3
α-helix	2741-2755	15
α-helix	2760-2765	6
α-helix	2766-2783	18
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	13
β-strand	2882-2883	2	13
α-helix	2886-2903	18
α-helix	2913-2926	14
β-strand	2932-2936	5	14
α-helix	2943-2953	11
α-helix	2956	1
β-strand	2957-2959	3	14
α-helix	2969-2980	12
α-helix	2981-2985	5
β-strand	2990-2995	6	14
α-helix	2996-2998	3
α-helix	3002-3014	13
α-helix	3024-3040	17
α-helix	3047-3061	15
β-strand	3062-3068	7	14
α-helix	3072-3081	10
α-helix	3084-3087	4
β-strand	3089-3093	5	14
α-helix	3097-3098	2
α-helix	3099-3109	11
α-helix	3120-3123	4
α-helix	3139-3164	26
α-helix	3173-3240	68
α-helix	3450-3481	32
α-helix	3483-3501	19
α-helix	3503-3516	14
α-helix	3522-3538	17
α-helix	3549-3552	4
α-helix	3556-3564	9
α-helix	3571-3581	11
α-helix	3586	1
β-strand	3587-3590	4	15
α-helix	3595-3603	9
β-strand	3610-3613	4	15
α-helix	3619-3629	11
β-strand	3632-3636	5	15
α-helix	3638-3640	3
α-helix	3643-3645	3
α-helix	3646-3650	5
β-strand	3653-3656	4	16
β-strand	3659-3664	6	16
β-strand	3667-3670	4	16
β-strand	3676-3681	6	15
α-helix	3690-3695	6
β-strand	3697-3700	4	15
α-helix	3702-3704	3
α-helix	3705-3720	16
α-helix	3722-3754	33
α-helix	3760-3762	3
α-helix	3764-3798	35
α-helix	3799-3801	3
α-helix	3802-3816	15
α-helix	3817-3820	4
α-helix	3829-3840	12
α-helix	3844-3846	3
α-helix	3852-3873	22
α-helix	3877-3879	3
α-helix	3880-3893	14
α-helix	3902-3910	9
α-helix	3929-3938	10
α-helix	3942-3944	3
α-helix	3947-3953	7
α-helix	3957-3961	5
α-helix	3979-3981	3
α-helix	3982-3996	15
α-helix	3998-4000	3
α-helix	4001-4013	13
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	4052-4061	10
β-strand	4066-4070	5	17
α-helix	4074-4090	17
β-strand	4093-4097	5	17
α-helix	4099-4101	3
α-helix	4103-4114	12
β-strand	4123-4129	7	17
α-helix	4136-4141	6
β-strand	4143-4147	5	17
α-helix	4153-4163	11
α-helix	4166-4169	4
α-helix	4176-4192	17
α-helix	4193-4195	3
α-helix	4197-4200	4
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
α-helix	4275-4278	4
β-strand	4283	1	18
β-strand	4295	1	18
α-helix	4302-4310	9
α-helix	4318-4321	4
α-helix	4325-4328	4
α-helix	4329-4345	17
α-helix	4375-4390	16
α-helix	4396-4400	5
α-helix	4408-4438	31
α-helix	4446-4456	11
α-helix	4462-4464	3
α-helix	4475-4497	23
α-helix	4500-4506	7
β-strand	4509-4510	2	19
α-helix	4517-4532	16
α-helix	4536-4538	3
β-strand	4539-4546	8	19
β-strand	4557-4561	5	19
β-strand	4564-4570	7	20
β-strand	4574-4584	11	20
β-strand	4587-4594	8	19
β-strand	4604-4610	7	20
β-strand	4618-4626	9	20
α-helix	4627	1
α-helix	4632-4637	6
β-strand	4641-4643	3	20

Chain B: 162 helices, 68 β-strands

Element	Residues	Length	Sheet
α-helix	1458-1472	15
β-strand	1474	1	21
β-strand	1476-1480	5	22
β-strand	1484-1488	5	22
α-helix	1490-1509	20
α-helix	1517-1548	32
α-helix	1549-1553	5
α-helix	1556-1560	5
α-helix	1562-1584	23
β-strand	1587	1	21
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	1647-1650	4
α-helix	1654-1656	3
β-strand	1663-1666	4	23
β-strand	1672-1677	6	23
β-strand	1683-1691	9	23
α-helix	1698-1724	27
α-helix	1735-1744	10
α-helix	1747-1768	22
α-helix	1775-1776	2
α-helix	1778-1795	18
α-helix	1802-1827	26
α-helix	1836-1839	4
β-strand	1842-1846	5	24
α-helix	1853-1855	3
β-strand	1857-1861	5	24
β-strand	1864-1867	4	24
α-helix	1876-1880	5
α-helix	1883-1897	15
β-strand	1901-1905	5	25
α-helix	1912-1922	11
β-strand	1927-1931	5	25
α-helix	1938-1951	14
β-strand	1954-1958	5	25
α-helix	1960-1962	3
α-helix	1965-1984	20
α-helix	1996-1997	2
β-strand	1998-2000	3	26
β-strand	2005-2007	3	26
β-strand	2013-2018	6	25
α-helix	2025-2029	5
α-helix	2030-2033	4
β-strand	2036-2040	5	25
α-helix	2046-2057	12
α-helix	2062-2079	18
α-helix	2090-2117	28
α-helix	2124-2129	6
α-helix	2133-2144	12
α-helix	2146-2148	3
α-helix	2153-2164	12
α-helix	2172-2174	3
α-helix	2176-2188	13
α-helix	2191-2193	3
α-helix	2201-2216	16
β-strand	2219-2223	5	27
α-helix	2230-2245	16
α-helix	2247-2248	2
β-strand	2249-2254	6	27
α-helix	2261-2265	5
β-strand	2266-2268	3	28
β-strand	2275-2277	3	28
α-helix	2279-2289	11
α-helix	2294-2296	3
β-strand	2298-2303	6	27
α-helix	2313-2315	3
α-helix	2316-2319	4
β-strand	2324-2326	3	29
β-strand	2332-2334	3	29
α-helix	2335-2336	2
β-strand	2339-2345	7	27
α-helix	2353-2358	6
β-strand	2360-2363	4	27
α-helix	2371-2384	14
α-helix	2411-2423	13
α-helix	2432-2440	9
α-helix	2451-2475	25
α-helix	2480-2482	3
α-helix	2483-2502	20
α-helix	2508-2521	14
α-helix	2534-2536	3
β-strand	2537-2539	3	30
β-strand	2545-2547	3	30
α-helix	2548-2551	4
α-helix	2559-2561	3
α-helix	2572-2586	15
β-strand	2591-2594	4	31
α-helix	2601-2609	9
β-strand	2615-2620	6	31
α-helix	2628-2638	11
β-strand	2639-2644	6	32
β-strand	2647-2652	6	32
β-strand	2658-2663	6	31
α-helix	2678-2688	11
β-strand	2691-2694	4	32
β-strand	2699-2703	5	32
β-strand	2706-2712	7	31
α-helix	2722-2724	3
α-helix	2725-2728	4
β-strand	2733-2735	3	31
α-helix	2737-2740	4
α-helix	2741-2755	15
α-helix	2760-2765	6
α-helix	2766-2783	18
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	33
β-strand	2882-2883	2	33
α-helix	2886-2903	18
α-helix	2913-2926	14
β-strand	2932-2936	5	34
α-helix	2943-2954	12
α-helix	2956	1
β-strand	2957-2959	3	34
α-helix	2969-2984	16
β-strand	2990-2995	6	34
α-helix	2996-2998	3
α-helix	3002-3014	13
α-helix	3024-3039	16
α-helix	3047-3061	15
β-strand	3062-3068	7	34
α-helix	3072-3081	10
α-helix	3084-3087	4
β-strand	3089-3093	5	34
α-helix	3099-3109	11
α-helix	3139-3163	25
α-helix	3173-3240	68
α-helix	3450-3481	32
α-helix	3483-3494	12
α-helix	3496-3501	6
α-helix	3503-3516	14
α-helix	3522-3538	17
α-helix	3549-3553	5
α-helix	3556-3564	9
α-helix	3571-3581	11
α-helix	3586	1
β-strand	3587-3590	4	35
α-helix	3595-3603	9
α-helix	3605-3607	3
β-strand	3610-3613	4	35
α-helix	3619-3629	11
β-strand	3633-3636	4	35
α-helix	3638-3640	3
α-helix	3646-3649	4
β-strand	3653-3654	2	36
β-strand	3661-3664	4	36
β-strand	3667-3670	4	36
α-helix	3671-3672	2
β-strand	3677-3681	5	35
α-helix	3690-3695	6
β-strand	3697-3700	4	35
α-helix	3702-3704	3
α-helix	3705-3720	16
α-helix	3722-3754	33
α-helix	3760-3762	3
α-helix	3764-3798	35
α-helix	3799-3801	3
α-helix	3802-3816	15
α-helix	3817-3820	4
α-helix	3829-3840	12
α-helix	3844-3846	3
α-helix	3852-3873	22
α-helix	3877-3879	3
α-helix	3880-3893	14
α-helix	3902-3910	9
α-helix	3911-3913	3
α-helix	3929-3938	10
α-helix	3942-3944	3
α-helix	3947-3952	6
α-helix	3957-3961	5
α-helix	3966-3969	4
α-helix	3979-3981	3
α-helix	3982-3996	15
α-helix	3998-4000	3
α-helix	4001-4013	13
α-helix	4019-4022	4
α-helix	4024-4025	2
α-helix	4027-4029	3
α-helix	4030-4034	5
β-strand	4041-4045	5	37
α-helix	4052-4062	11
β-strand	4066-4070	5	37
α-helix	4074-4090	17
β-strand	4093-4097	5	37
α-helix	4099-4101	3
α-helix	4103-4114	12
β-strand	4123-4129	7	37
α-helix	4136-4141	6
β-strand	4143-4147	5	37
α-helix	4153-4163	11
α-helix	4166-4169	4
α-helix	4176-4192	17
α-helix	4197-4200	4
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
α-helix	4275-4278	4
β-strand	4283-4285	3	38
β-strand	4294-4295	2	38
α-helix	4296-4297	2
α-helix	4302-4310	9
α-helix	4318-4321	4
α-helix	4325-4328	4
α-helix	4329-4345	17
α-helix	4375-4390	16
α-helix	4402-4405	4
α-helix	4408-4438	31
α-helix	4446-4456	11
α-helix	4476-4497	22
α-helix	4501-4506	6
β-strand	4509-4510	2	39
α-helix	4517-4531	15
α-helix	4536-4538	3
β-strand	4539-4546	8	39
β-strand	4557-4561	5	39
β-strand	4564-4571	8	40
β-strand	4574-4584	11	40
β-strand	4587-4594	8	39
β-strand	4604-4610	7	40
β-strand	4618-4626	9	40
α-helix	4627	1
α-helix	4632-4637	6
β-strand	4641-4643	3	40

Chain C: 4 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	96-104	9	41
β-strand	111-116	6	42
β-strand	123-127	5	42
β-strand	131-136	6	42
β-strand	141-147	7	42
β-strand	153-158	6	43
β-strand	164-169	6	43
β-strand	174-178	5	43
β-strand	183-188	6	43
β-strand	195-200	6	44
β-strand	206-211	6	44
β-strand	215-220	6	44
β-strand	226-231	6	44
β-strand	237-242	6	45
β-strand	248-253	6	45
β-strand	258-262	5	45
β-strand	268-272	5	45
β-strand	279-284	6	46
α-helix	285-286	2
α-helix	287-289	3
α-helix	290-297	8
α-helix	299-302	4
β-strand	310-315	6	46
β-strand	319-324	6	46
β-strand	329-335	7	46
β-strand	341-346	6	47
β-strand	353-357	5	47
β-strand	361-366	6	47
β-strand	371-377	7	47
β-strand	383-388	6	41
β-strand	394-399	6	41
β-strand	404-409	6	41

Chain D: 3 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	96-104	9	48
β-strand	111-116	6	49
β-strand	123-127	5	49
β-strand	132-136	5	49
β-strand	141-146	6	49
β-strand	153-158	6	50
β-strand	164-169	6	50
β-strand	174-178	5	50
β-strand	183-188	6	50
β-strand	195-200	6	51
β-strand	206-211	6	51
β-strand	215-220	6	51
β-strand	228-231	4	51
β-strand	237-242	6	52
β-strand	248-253	6	52
β-strand	258-262	5	52
β-strand	270-272	3	52
β-strand	279-282	4	53
α-helix	287-289	3
α-helix	290-297	8
α-helix	299-301	3
β-strand	310-315	6	53
β-strand	319-324	6	53
β-strand	330-335	6	53
β-strand	341-346	6	54
β-strand	352-357	6	54
β-strand	361-366	6	54
β-strand	373-377	5	54
β-strand	383-388	6	48
β-strand	394-399	6	48
β-strand	404-409	6	48

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytoplasmic dynein 1 heavy chain 1	A, B	protein	4646	Homo sapiens	Q14204
Platelet-activating factor acetylhydrolase IB subunit beta	C, D	protein	410	Homo sapiens	P43034 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9E11_1 Cytoplasmic dynein 1 heavy chain 1 (chains A, B)
MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKS
ALEQMRKFLSDPQVHTVLVERSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIK
RTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPFFKSYIRESGKADRDGDKMAP
SVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLT
LDILKHGKRFHATVSFDTDTGLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAI
FTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRKLMHVAYEEFEKVMVACFEVF
QTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSK
EGTEAWEAAMKRYDERIDRVETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGA
IREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRDLPPVSGSIIWAKQIDRQLTA
YMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAIS
LIESVRTYERTCEKVEERNTISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETV
FNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNRVQKAVDDLNLHSYSNLPIWV
NKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYR
NALTRMPDGPVALEESYSAVMGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQ
ALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKYDSWHKEVLSKFGQMLGSNMT
EFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTD
WEKTKPVTGNLRPEEALQALTIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQ
VALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLRQNLDALLNQLKSFPARLRQY
ASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEH
INSVSAMKLSPYYKVFEEDALSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHL
LPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRSLERLADLLGKIQKALGEYLE
RERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYIT
WIDKYQAQLVVLSAQIAWSENVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQ
PPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLSQMRFYFDPKQTDVLQQLSIQ
MANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQE
ALREHSNPNYDKTSAPITCELLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLA
MTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQLSSQSHYDFGLRALKSVLVSA
GNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGL
MMVGPSGSGKSMAWRVLLKALERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLF
THVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLDDNKLLTLPNGERLSLPPNVR
IMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFS
MLHQACRNVAQYNANHPDFPMQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRR
ITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETHKVAAPDVVVPTLDTVRHEAL
LYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTW
VKLERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIP
SLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMTRWVRGIFEALRPLETLPVEG
LIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSG
AGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVL
DSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLMLDSHEELYKWFTSQVIR
NLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFI
NHYANLFHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKL
KKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIK
KQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLE
DDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLK
SLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQMRQNLFTTWSHHLQQAN
IQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRV
LITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAE
RPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEV
TRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPT
YDAEFQHFLRGNEIVLSAGSTPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIW
LDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDRLLAMAHMFVSTNLGESFMSI
MEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLR
AGRIFVFEPPPGVKANMLRTFSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLG
WSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPWSALKTLMAQSIYGGRVDNEF
DQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTL
HTTASNWLHLIPQTLSHLKRTVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEG
KKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQLQNISLAAASGG
AKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIF
TVDFEIATKEDPRSFYERGVAVLCTE

Sequence of entity 2 (C, D), FASTA

>9E11_2 Platelet-activating factor acetylhydrolase IB subunit beta (chains C, D)
MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDVNEELDKKYAGLLEKKWTSVIR
LQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVF
SVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQ
GFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSE
TKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDK
TLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR

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

Nde1 promotes Lis1 binding to full-length autoinhibited human dynein 1. Yang, J., Zhao, Y., Chai, P. et al. Nat Chem Biol (2026) 22:274-283. DOI 10.1038/s41589-025-01981-6 · 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+
9E0X 2.7 Å, Cryo-EM structure of Phi dynein
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

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