27QB: Dynein heavy chain, cytoplasmic

Dictyostelium discoideum cytoplasmic dynein motor domain in the absence of nucleotide (Apo state 2). Determined by electron microscopy at 2.66 Å resolution. Released 26 Aug 2026.

Method
Electron microscopy
Resolution
2.66 Å
Organism
Dictyostelium discoideum AX2
Chains
1
Atoms
24,394
Mol. weight
384.86 kDa
Ligands
ATP, MG
Released
26 Aug 2026

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

Secondary structure: helices and β-sheets

27QB contains 176 α-helices and 74 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: 176 helices, 74 β-strands

ElementResiduesLengthSheet
α-helix1402-141514
β-strand141811
α-helix1419-14213
α-helix1424-143714
α-helix1443-14464
α-helix1449-14513
α-helix1452-146312
α-helix1465-14717
α-helix1478-14858
β-strand149811
α-helix1499-15013
α-helix1505-15095
α-helix1511-153828
β-strand154212
β-strand1544-154853
β-strand1552-155653
α-helix1558-157417
α-helix1575-15773
α-helix1581-15844
α-helix1585-161935
α-helix1625-16284
α-helix1630-165122
β-strand165512
α-helix1656-16605
α-helix1665-169329
α-helix1695-16995
α-helix1702-17109
α-helix1716-17216
α-helix1722-17254
β-strand1729-173464
β-strand1740-174674
β-strand1751-175994
α-helix1766-179227
α-helix1800-18089
α-helix1812-183120
α-helix1838-186225
α-helix1869-189325
α-helix1904-19074
β-strand1911-191445
α-helix1921-19233
β-strand1925-192955
β-strand1932-193545
α-helix1946-19483
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-helix2105-211511
α-helix2121-213818
α-helix2149-216517
α-helix2171-21744
α-helix2177-220226
α-helix2204-22063
α-helix2211-222212
α-helix2229-22313
α-helix2234-224613
α-helix2253-226816
β-strand2271-227558
α-helix2282-229716
β-strand2300-230678
α-helix2308-23103
α-helix2313-23164
β-strand2318-232039
α-helix2323-23253
α-helix23261
β-strand2327-232939
α-helix2331-234010
α-helix2346-23483
β-strand2349-235688
α-helix2361-23644
α-helix2365-23673
α-helix2368-23714
β-strand2376-2378310
β-strand2384-2386310
α-helix2387-23882
β-strand2391-239778
α-helix2405-24095
β-strand2412-241548
α-helix2423-243614
α-helix2441-245616
α-helix2490-250213
α-helix2511-252111
α-helix2530-255425
α-helix2559-25613
α-helix2562-258019
α-helix2587-259913
α-helix2612-26143
β-strand2615-2617311
β-strand2624-2626311
α-helix2627-26304
α-helix2632-26332
α-helix2638-26403
α-helix2651-266414
β-strand2670-2672312
α-helix2680-26878
α-helix2688-26903
β-strand2694-2700712
α-helix2707-271711
β-strand2718-2722513
β-strand2728-2732513
β-strand2738-2744712
α-helix2750-27512
α-helix2758-276710
α-helix2768-27703
β-strand2771-2774413
β-strand2779-2783513
β-strand2786-2791612
α-helix2802-28043
α-helix2805-28084
β-strand2813-2814212
α-helix2821-283515
α-helix2836-28383
α-helix2840-28456
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-helix2965-298319
α-helix2987-29893
α-helix2992-300514
β-strand3012-3016515
α-helix3022-303312
β-strand3036-3038315
α-helix3048-305912
α-helix3060-30645
β-strand3069-3073515
α-helix3081-309313
α-helix3103-311816
α-helix3126-314015
β-strand3141-3147715
α-helix3162-31676
β-strand3169-3173515
α-helix3175-31773
α-helix3178-318811
α-helix3203-32119
α-helix3223-324927
α-helix3257-331054
α-helix3558-360043
α-helix3602-36043
α-helix3607-362317
α-helix3634-36374
α-helix3641-36499
α-helix3656-36649
α-helix36711
β-strand3672-3675416
α-helix3680-36889
β-strand3695-3698416
α-helix3704-371411
β-strand3717-3721516
α-helix3723-37253
α-helix3728-37303
α-helix3731-37344
β-strand3738-3740317
β-strand3745-3749517
β-strand3752-3755417
β-strand3761-3766616
α-helix3775-37784
β-strand3782-3785416
α-helix3787-37893
α-helix3790-380516
α-helix3807-38115
α-helix3812-38143
α-helix3819-384022
α-helix3845-38506
α-helix3852-388534
α-helix3887-390216
α-helix3903-39053
α-helix3913-392412
α-helix3928-39303
α-helix3936-395520
α-helix3961-397616
α-helix3982-39843
α-helix3985-39939
α-helix3998-40003
α-helix4006-40083
α-helix4014-402613
α-helix4028-40303
α-helix4033-40397
α-helix4045-40484
α-helix4057-40593
α-helix4060-406910
α-helix4075-408915
α-helix4091-40933
α-helix4094-410512
α-helix4118-41203
α-helix4121-41255
β-strand4132-4136518
α-helix4143-415311
β-strand4157-4161518
α-helix4166-418116
β-strand4184-4188518
α-helix4190-41923
α-helix4194-420512
β-strand4214-4220718
α-helix4227-42326
β-strand4234-4238518
α-helix4240-42423
α-helix4244-425310
α-helix4257-42604
α-helix4266-428318
α-helix4284-42874
α-helix4300-431819
α-helix4331-43377
α-helix4338-43436
α-helix4350-436314
α-helix4366-43694
β-strand4374-4376319
β-strand4381-4382219
α-helix4389-43979
α-helix4405-44084
α-helix4414-443219
α-helix4461-447616
α-helix4479-44846
α-helix4494-452330
α-helix4524-45263
α-helix4532-454312
α-helix4545-45473
α-helix4561-457919
β-strand4589-4590220
α-helix4591-45933
α-helix4597-461216
α-helix4616-46183
β-strand4619-4626820
β-strand4636-4640520
β-strand4642-4645421
β-strand4648-4650322
β-strand4653-4655322
β-strand4661-4664421
β-strand4667-4673720
α-helix4677-46793
α-helix4682-46843
β-strand4686-4691621
β-strand4699-4705721
β-strand4707122
α-helix4713-47197
β-strand4722-4724321

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Dynein heavy chain, cytoplasmicAprotein3367Dictyostelium discoideum AX2P34036
Sequence of entity 1 (A), FASTA
>27QB_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
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P31
MGMagnesium ionMg1

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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