27QA: Dynein heavy chain, cytoplasmic

Dictyostelium discoideum cytoplasmic dynein motor domain in the presence of ADP (Apo state 1). Determined by electron microscopy at 2.76 Å resolution. Released 26 Aug 2026.

Method
Electron microscopy
Resolution
2.76 Å
Organism
Dictyostelium discoideum AX2
Chains
1
Atoms
24,612
Mol. weight
385.72 kDa
Ligands
ADP, MG, ATP
Released
26 Aug 2026

Explore 27QA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

27QA contains 158 α-helices and 73 β-strands across 1 chain. 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: 158 helices, 73 β-strands

ElementResiduesLengthSheet
α-helix1401-141515
β-strand141811
α-helix1419-14213
α-helix1424-143916
α-helix1443-14464
α-helix1449-147224
α-helix1478-148811
β-strand149811
α-helix1499-15035
α-helix1507-154034
β-strand154212
β-strand1544-154853
β-strand1552-155653
α-helix1558-157518
α-helix1585-161935
α-helix1625-16284
α-helix1630-165223
β-strand165512
α-helix1656-16605
α-helix1665-169329
α-helix1695-16995
α-helix1702-17109
α-helix1715-17184
α-helix1719-17213
α-helix1722-17254
β-strand1729-173464
β-strand1740-174674
β-strand1751-175994
α-helix1766-179328
α-helix1800-180910
α-helix1812-183120
α-helix1838-186326
α-helix1869-189426
α-helix1904-19074
β-strand1910-191455
α-helix1921-19233
β-strand1925-192955
β-strand1932-193545
α-helix1944-19485
α-helix1951-196515
β-strand1969-197356
α-helix1980-199011
β-strand1995-199956
α-helix2006-201914
β-strand2022-202656
α-helix2028-20303
α-helix2033-205119
β-strand2056-205727
β-strand2065-206627
β-strand2072-207546
β-strand207716
α-helix2089-20924
β-strand2095-209956
α-helix21011
α-helix21031
α-helix2105-211511
α-helix2121-213818
α-helix2149-216517
α-helix2171-21733
α-helix2177-220226
α-helix2204-22063
α-helix2211-222212
α-helix2229-22324
α-helix2234-224613
α-helix2253-226816
β-strand2271-227558
α-helix2282-229716
β-strand2300-230678
α-helix2313-23175
β-strand2318-232149
β-strand2326-232949
α-helix2331-234111
α-helix2346-23483
β-strand2349-235688
α-helix2361-237111
β-strand2376-2378310
α-helix23791
β-strand2384-2386310
β-strand2391-239778
α-helix2405-24084
β-strand2412-241548
α-helix2423-243614
α-helix2441-245616
α-helix2490-250617
α-helix2511-252111
α-helix2530-255425
α-helix2562-258221
α-helix2587-260014
α-helix2612-26143
β-strand2615-2618411
β-strand2623-2626411
α-helix2627-26293
α-helix2651-266515
β-strand2670-2673412
α-helix2680-268910
β-strand2694-2700712
α-helix2707-271711
β-strand2718-2722513
α-helix27231
β-strand2728-2732513
β-strand2738-2744712
α-helix2750-27512
α-helix2758-276811
β-strand2771-2774413
β-strand2779-2783513
β-strand2786-2792712
α-helix2802-28043
α-helix2805-28084
β-strand2813-2815312
α-helix2821-283515
α-helix2836-28383
α-helix2846-286318
α-helix2876-289217
α-helix2898-290912
α-helix2910-29145
α-helix2920-293718
α-helix2943-29464
β-strand2952-2953214
β-strand2961-2962214
α-helix2965-298218
α-helix2992-300514
β-strand3012-3016515
α-helix3022-303211
β-strand3036-3038315
α-helix3048-306417
β-strand3069-3074615
α-helix3075-30773
α-helix3081-309212
α-helix3102-311918
α-helix3126-314015
β-strand3142-3147615
α-helix3163-31664
β-strand3169-3174615
α-helix3178-318811
α-helix3203-32119
α-helix3223-324927
α-helix3257-331357
α-helix3544-356926
α-helix3573-358614
α-helix3588-360114
α-helix3607-362317
α-helix3634-36374
α-helix3641-36499
α-helix3656-366611
β-strand3671-3675516
α-helix3680-36889
α-helix3690-36923
β-strand3695-3698416
α-helix3704-371411
β-strand3717-3721516
α-helix3723-37253
α-helix3728-37303
α-helix3731-37355
β-strand3739-3741317
β-strand3744-3749617
β-strand3752-3755417
β-strand3761-3766616
α-helix3775-37784
β-strand3781-3785516
α-helix3789-380517
α-helix3807-384135
α-helix3849-390254
α-helix3903-39053
α-helix3913-392513
α-helix3928-39303
α-helix3936-395520
α-helix3961-397616
α-helix3982-39843
α-helix3985-39928
α-helix4006-40083
α-helix4014-402613
α-helix4028-40303
α-helix4033-40397
α-helix4041-40444
α-helix4055-40562
α-helix4060-406910
α-helix4075-408915
α-helix4091-40933
α-helix4094-410613
α-helix4118-41203
α-helix4121-41255
β-strand4132-4136518
α-helix4143-415311
β-strand4157-4161518
α-helix4165-41673
α-helix4170-418112
β-strand4184-4188518
α-helix4190-41923
α-helix4194-420512
β-strand4214-4220718
α-helix4227-42315
β-strand4234-4238518
α-helix4240-42423
α-helix4244-42529
α-helix4257-42604
α-helix4265-428319
α-helix4284-42874
α-helix4300-431617
α-helix4326-43283
α-helix4331-43366
α-helix4337-43437
α-helix4350-436314
α-helix4366-43694
β-strand4374-4376319
β-strand4381-4382219
α-helix4389-43979
α-helix4405-44084
α-helix4413-443220
α-helix4461-447313
α-helix4474-44763
α-helix4477-44815
α-helix4490-44923
α-helix4494-452532
α-helix4532-454211
α-helix4561-457919
β-strand4588-4590320
α-helix4591-45933
α-helix4597-461216
α-helix4616-46183
β-strand4619-4626820
β-strand4636-4640520
β-strand4643-4645321
β-strand4648-4650322
β-strand4653-4655322
β-strand4661-4663321
β-strand4667-4673720
α-helix4677-46848
β-strand4686-4691621
β-strand4699-4705721
α-helix4713-47186
β-strand4722-4724321

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Dynein heavy chain, cytoplasmicAprotein3367Dictyostelium discoideum AX2P34036
Sequence of entity 1 (A), FASTA
>27QA_1 Dynein heavy chain, cytoplasmic (chains A)
MTRHHHHHHGGGDYKDDDDKGGGKVPVEEEIQDLKAVWVELSNTWQEIDSLKETAWSAII
PRKVRKSLEDTLQKLKNLPNRIRQYSAFDHAQNLIKIYLKGNAIITDLHSEAIKDRHWKI
LKKRLNTNWIITELTLGSIWDSDLARNENIYREVITAAQGEIALEEFLKGVREFWTTLEL
DLVNYQRKCKLVRGWDDLFNKLAEHLNSISAMKMSPYYKVFEEEANHWDDRLNKVRSLLD
VWIDVQRRWVYLEGIFSGSGDINQLLPAESTRFKSINSEFIAILKKVSGAPLILEVLAIE
RIQQTMERLSDLLGKVQKALGEYLERQRSAFARFYFVGDEDLLEIIGNSKDIIKIQKHFR
KMFAGLANLTLDDEKTTIIGMSSAEGETVTFKKPISIANGPKIHEWLTMVESEMKSTLAT
LLSESLQHFNQVDVNDHSKYSEWVDNYPTQLVLLTSQIVWSTQVDQALGGGTLQQSKIQE
QLQSIEQTTQMILNNLADSVLQDLSAQKRKKFEHLITELVHQRDVVRQLQKCKNLTGNKD
FDWLYHMRYYYDATQENVLHKLVIHMANATFYYGFEYLGIGERLVQTPLTDRCYLTLTQA
LESRMGGNPFGPAGTGKTETVKALGSQLGRFVLVFCCDEGFDLQAMSRIFVGLCQCGAWG
CFDEFNRLEERILSAVSQQIQTIQVALKENSKEVELLGGKNISLHQDMGIFVTMNPGYAG
RSNLPDNLKKLFRSMAMIKPDREMIAQVMLYSQGFKTAEVLAGKIVPLFKLCQEQLSAQS
HYDFGLRALKSVLVSAGGIKRKCQPPQLPPITDAESKTKADQIYCQYEIGVLLNSINDTM
IPKLVADDIPLIQSLLLDVFPGSQLQPIQMDQLRKKIQEIAKQRHLVTKQEWVEKILQLH
QILNINHGVMMVGPSGGGKTTSWEVYLEAIEQVDNIKSEAHVMDPKAITKDQLFGSLDLT
TREWTDGLFTATLRRIIDNVRGESTKRHWIIFDGDVDPEWVENLNSLLDDNKLLTLPNGE
RLALPNNVRVMFEVQDLKYATLATISRCGMVWFSEEILTTQMIFQNYLDTLSNEPFDPQE
KEQQKRNENAQLQQQQQTTITSPILTSPPTTSSSSRSTTSTTSMIPAGLKVQKECAAIIS
QYFEPGGLVHKVLEDAGQRPHIMDFTRLRVLNSFFSLMNRSIVNVIEYNQLHSDFPMSPE
NQSNYITNRLLYSLMWGLGGSMGLVERENFSKFIQTIAITPVPANTIPLLDYSVSIDDAN
WSLWKNKVPSVEVETHKVASPDVVIPTVDTTRHVDVLHAWLSEHRPLILCGPPGSGKTMT
LTSTLRAFPDFEVVSLNFSSATTPELLLKTFDHHCEYKRTPSGETVLRPTQLGKWLVVFC
DEINLPSTDKYGTQRVITFIRQMVEKGGFWRTSDHTWIKLDKIQFVGACNPPTDAGRVQL
THRFLRHAPILLVDFPSTSSLTQIYGTFNRALMKLLPNLRSFADNLTDAMVEFYSESQKR
FTPDIQAHYIYSPRELSRWDRALLEAIQTMDGCTLEGLVRLWAHEALRLFQDRLVETEEK
EWTDKKIDEVALKHFPSVNLDALKRPILYSNWLTKDYQPVNRSDLREYVKARLKVFYEEE
LDVPLVLFNEVLDHILRIDRVFRQPQGHALLIGVSGGGKSVLSRFVAWMNGLSIYTIKVN
NNYKSSDFDDDLRMLLKRAGCKEEKICFIFDESNVLESSFLERMNTLLAGGEVPGLFEGE
EFTALMHACKETAQRNGLILDSEEELYKYFTSQVRRNLHVVFTMNPASPDFHNRSATSPA
LFNRCVLDWFGEWSPEALFQVGSEFTRNLDLENPQYIAPPVFIQEAEIMGNNLMAIPPSH
RDAVVSSLVYIHQTIGEANIRLLKRQGRQNYVTPRHYLDFINQVVLLINEKRDQLEEEQL
HLNIGLKKLRDTEAQVKDLQVSLAQKNRELDVKNEQANQKLKQMVQDQQAAEIKQKDARE
LQVQLDVRNKEIAVQKVKAYADLEKAEPAIIEAQEAVSTIKKKHLDEIKSLPKPPTPVKL
AMEAVCLMLGGKKLEWADIRKKIMEPNFITSIINYDTKKMMTPKIREAITKGYLEDPGFD
YETVNRASKACGPLVKWATAQTYYSEILDRIKPLREEVEQLENAANELKLKQDEIVATIT
ALEKSIATYKEEYATLIRETEQIKTESSKVKNKVDRSIALLDNLNSERGRWEQQSENFNT
QMSTVVGDVVLASAFLAYIGFFDQNFRTDLMRKWMIRLDSVGIKFKSDLSVPSFLSKPEE
RLNWHANSLPSDELCIENAIMLKRFNRYPLVIDPSGQAMEFLMNQYADKKITKTSFLDSS
FMKNLESALRFGCPLLVQDVENIDPVLNPVLNKEIRKKGGRILIRLGDQDVDFSPSFMIF
LFTRDPTAHFTPDLCSRVTFVNFTVTPSSLQSQCLHEALKTERPDTHKKRSDLLKIQGEF
QVKLRILEKSLLNALSQASGNILDDDSVISTLETLKKETTEIALKVEETETVMQEISEVS
ALYNPMALSCSRVYFAMEELSQFHLYQFSLRAFLDIFYNLLNNNPNLVDKKDPNERLVYL
SKDIFSMTFNRVTRTLLNDDKLTFALQLTIISVKGTSNEIEESEWDFLLKGGDNLTSIKE
TIPQLDSLLSTTQQKWLICLRQQVPSFSKLVDHIQQNSSDWKQFFGKDQVGEPIIPESWI
VAQAQLSNQQSTIVSNFRKILLMKAFHSDRVLQYSHSFVCSVFGEDFLNTQELDMANIVE
KEVKSSSPLLLCSVPGYDASSKVDDLALQLHKQYKSFAIGSPEGFELAEKSIYAAAKSGT
WVLLKNIHLAPQWLVQLEKKLHSLSPHPSFRLFMTSEIHPALPANLLRMSNVFSYENPPG
VKANLLHTFIGIPATRMDKQPAERSRIYFLLAWFHAIIQERLRYIPLGWTKFFEFNDADL
RGALDSIDYWVDLYSKGRSNIDPDKIPWIAVRTILGSTIYGGRIDNEFDMRLLYSFLEQL
FTPSAFNPDFPLVPSIGLSVPEGTTRAHFMKWIEALPEISTPIWLGLPENAESLLLSNKA
RKMINDLQKMQSSEEDGEDDQVSGSSKKESSSSSSEDKGKAKLRATITEWTKLLPKPLKQ
LKRTTQNIKDPLFRCFEREISTGGKLVKKITNDLANLLELISGNIKSTNYLRSLTTSISK
GIVPKEWKWYSVPETISLSVWISDFSKRMQQLSEISESSDYSSIQVWLGGLLNPEAYITA
TRQSASQLNGWSLENLRLHASSLGKISSEGGASFNVKGMALEGAVWNNDQLTPTDILSTP
ISIATLTWKDKDDPIFNNSSSKLSVPVYLNETRSELLFSIDLPYDQSTSKQNWYQRSVSI
SSWKSDI

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P22
MGMagnesium ionMg1
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P31

Primary citation

ADP-Bound States of Cytoplasmic Dynein: Cryo-electron Microscopy Reveals a Two-Step Post-Power-Stroke Transition and Roles of Regulatory ATPase Sites. Imai, H., Kanazawa, R., Maeshima, T. et al. J Mol Biol (2026) 438:169977-169977. DOI 10.1016/j.jmb.2026.169977 · PubMed

Other PDB entries of the same protein (UniProt P34036), best resolution first:

Browse structure collections

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