Dictyostelium discoideum cytoplasmic dynein motor domain in complex with ADP.Vi (Phi-particle). Determined by electron microscopy at 2.2 Å resolution. Released 26 Aug 2026.
Explore 27PT in 3D Show helices and sheets RCSB PDB PDBe
27PT contains 164 α-helices and 71 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1514-1539 | 26 | |
| β-strand | 1542 | 1 | 1 |
| β-strand | 1545-1548 | 4 | 2 |
| β-strand | 1552-1555 | 4 | 2 |
| α-helix | 1558-1574 | 17 | |
| α-helix | 1575-1577 | 3 | |
| α-helix | 1588-1619 | 32 | |
| α-helix | 1624-1628 | 5 | |
| α-helix | 1630-1651 | 22 | |
| β-strand | 1655 | 1 | 1 |
| α-helix | 1656-1661 | 6 | |
| α-helix | 1665-1690 | 26 | |
| α-helix | 1695-1699 | 5 | |
| α-helix | 1702-1710 | 9 | |
| α-helix | 1715-1717 | 3 | |
| α-helix | 1719-1721 | 3 | |
| α-helix | 1722-1725 | 4 | |
| β-strand | 1731-1734 | 4 | 3 |
| β-strand | 1740-1745 | 6 | 3 |
| β-strand | 1751-1759 | 9 | 3 |
| α-helix | 1766-1792 | 27 | |
| α-helix | 1800-1808 | 9 | |
| α-helix | 1812-1831 | 20 | |
| α-helix | 1838-1863 | 26 | |
| α-helix | 1869-1893 | 25 | |
| α-helix | 1904-1907 | 4 | |
| β-strand | 1911-1914 | 4 | 4 |
| α-helix | 1921-1923 | 3 | |
| β-strand | 1925-1929 | 5 | 4 |
| β-strand | 1932-1935 | 4 | 4 |
| α-helix | 1951-1965 | 15 | |
| β-strand | 1969-1973 | 5 | 5 |
| α-helix | 1980-1990 | 11 | |
| β-strand | 1995-1999 | 5 | 5 |
| α-helix | 2006-2019 | 14 | |
| β-strand | 2022-2026 | 5 | 5 |
| α-helix | 2028-2030 | 3 | |
| α-helix | 2033-2051 | 19 | |
| β-strand | 2056-2060 | 5 | 6 |
| β-strand | 2063-2066 | 4 | 6 |
| β-strand | 2072-2077 | 6 | 5 |
| α-helix | 2085-2088 | 4 | |
| α-helix | 2089-2092 | 4 | |
| β-strand | 2095-2099 | 5 | 5 |
| α-helix | 2105-2115 | 11 | |
| α-helix | 2121-2138 | 18 | |
| α-helix | 2149-2165 | 17 | |
| α-helix | 2168-2173 | 6 | |
| α-helix | 2179-2202 | 24 | |
| α-helix | 2204-2206 | 3 | |
| α-helix | 2209-2211 | 3 | |
| α-helix | 2212-2222 | 11 | |
| α-helix | 2230-2232 | 3 | |
| α-helix | 2234-2246 | 13 | |
| α-helix | 2253-2268 | 16 | |
| β-strand | 2271-2275 | 5 | 7 |
| α-helix | 2282-2297 | 16 | |
| β-strand | 2301-2306 | 6 | 7 |
| α-helix | 2313-2317 | 5 | |
| β-strand | 2318-2320 | 3 | 8 |
| β-strand | 2327-2329 | 3 | 8 |
| α-helix | 2331-2341 | 11 | |
| α-helix | 2346-2348 | 3 | |
| β-strand | 2350-2356 | 7 | 7 |
| α-helix | 2361-2364 | 4 | |
| α-helix | 2365-2367 | 3 | |
| α-helix | 2368-2371 | 4 | |
| β-strand | 2376-2378 | 3 | 9 |
| β-strand | 2384-2386 | 3 | 9 |
| α-helix | 2387-2388 | 2 | |
| β-strand | 2391-2397 | 7 | 7 |
| α-helix | 2405-2410 | 6 | |
| β-strand | 2412-2415 | 4 | 7 |
| α-helix | 2423-2436 | 14 | |
| α-helix | 2441-2459 | 19 | |
| α-helix | 2490-2502 | 13 | |
| α-helix | 2503-2506 | 4 | |
| α-helix | 2511-2520 | 10 | |
| α-helix | 2530-2554 | 25 | |
| α-helix | 2559-2561 | 3 | |
| α-helix | 2562-2582 | 21 | |
| α-helix | 2587-2600 | 14 | |
| α-helix | 2612-2614 | 3 | |
| β-strand | 2615-2617 | 3 | 10 |
| β-strand | 2624-2626 | 3 | 10 |
| α-helix | 2627-2630 | 4 | |
| α-helix | 2638-2640 | 3 | |
| α-helix | 2651-2665 | 15 | |
| β-strand | 2671-2673 | 3 | 11 |
| α-helix | 2680-2688 | 9 | |
| β-strand | 2694-2700 | 7 | 11 |
| α-helix | 2707-2717 | 11 | |
| β-strand | 2718-2722 | 5 | 12 |
| β-strand | 2728-2732 | 5 | 12 |
| β-strand | 2738-2744 | 7 | 11 |
| α-helix | 2750-2751 | 2 | |
| α-helix | 2758-2768 | 11 | |
| β-strand | 2771-2774 | 4 | 12 |
| β-strand | 2779-2783 | 5 | 12 |
| β-strand | 2786-2792 | 7 | 11 |
| α-helix | 2802-2804 | 3 | |
| α-helix | 2805-2808 | 4 | |
| β-strand | 2813-2815 | 3 | 11 |
| α-helix | 2821-2836 | 16 | |
| α-helix | 2840-2842 | 3 | |
| α-helix | 2846-2863 | 18 | |
| α-helix | 2876-2890 | 15 | |
| α-helix | 2898-2913 | 16 | |
| α-helix | 2920-2937 | 18 | |
| α-helix | 2943-2946 | 4 | |
| α-helix | 2947 | 1 | |
| α-helix | 2949 | 1 | |
| β-strand | 2952-2953 | 2 | 13 |
| β-strand | 2961-2962 | 2 | 13 |
| α-helix | 2965-2982 | 18 | |
| α-helix | 2992-3005 | 14 | |
| β-strand | 3012-3015 | 4 | 14 |
| α-helix | 3022-3032 | 11 | |
| β-strand | 3036-3038 | 3 | 14 |
| α-helix | 3048-3063 | 16 | |
| β-strand | 3069-3074 | 6 | 14 |
| α-helix | 3075-3077 | 3 | |
| α-helix | 3081-3093 | 13 | |
| α-helix | 3103-3118 | 16 | |
| α-helix | 3126-3140 | 15 | |
| β-strand | 3141-3147 | 7 | 14 |
| α-helix | 3154-3156 | 3 | |
| α-helix | 3163-3166 | 4 | |
| β-strand | 3169-3172 | 4 | 14 |
| α-helix | 3174 | 1 | |
| α-helix | 3176-3177 | 2 | |
| α-helix | 3178-3188 | 11 | |
| α-helix | 3203-3212 | 10 | |
| α-helix | 3223-3249 | 27 | |
| α-helix | 3257-3313 | 57 | |
| α-helix | 3546-3566 | 21 | |
| α-helix | 3568-3586 | 19 | |
| α-helix | 3588-3601 | 14 | |
| α-helix | 3602-3604 | 3 | |
| α-helix | 3607-3623 | 17 | |
| α-helix | 3634-3638 | 5 | |
| α-helix | 3641-3649 | 9 | |
| α-helix | 3656-3664 | 9 | |
| α-helix | 3671 | 1 | |
| β-strand | 3672-3675 | 4 | 15 |
| α-helix | 3680-3688 | 9 | |
| α-helix | 3690-3692 | 3 | |
| β-strand | 3695-3698 | 4 | 15 |
| α-helix | 3704-3714 | 11 | |
| β-strand | 3717-3721 | 5 | 15 |
| α-helix | 3723-3725 | 3 | |
| α-helix | 3728-3730 | 3 | |
| α-helix | 3731-3735 | 5 | |
| β-strand | 3738-3741 | 4 | 16 |
| β-strand | 3744-3748 | 5 | 16 |
| β-strand | 3753-3755 | 3 | 16 |
| β-strand | 3761-3766 | 6 | 15 |
| α-helix | 3775-3780 | 6 | |
| β-strand | 3782-3785 | 4 | 15 |
| α-helix | 3790-3805 | 16 | |
| α-helix | 3807-3839 | 33 | |
| α-helix | 3849-3883 | 35 | |
| α-helix | 3887-3902 | 16 | |
| α-helix | 3903-3905 | 3 | |
| α-helix | 3913-3925 | 13 | |
| α-helix | 3928-3930 | 3 | |
| α-helix | 3936-3955 | 20 | |
| α-helix | 3961-3976 | 16 | |
| α-helix | 3982-3984 | 3 | |
| α-helix | 3985-3993 | 9 | |
| α-helix | 3998-4000 | 3 | |
| α-helix | 4006-4008 | 3 | |
| α-helix | 4014-4026 | 13 | |
| α-helix | 4028-4030 | 3 | |
| α-helix | 4033-4039 | 7 | |
| α-helix | 4041-4048 | 8 | |
| α-helix | 4060-4069 | 10 | |
| α-helix | 4075-4088 | 14 | |
| α-helix | 4094-4106 | 13 | |
| α-helix | 4118-4120 | 3 | |
| α-helix | 4121-4125 | 5 | |
| β-strand | 4132-4136 | 5 | 17 |
| α-helix | 4143-4153 | 11 | |
| β-strand | 4157-4161 | 5 | 17 |
| β-strand | 4162 | 1 | 18 |
| β-strand | 4164 | 1 | 18 |
| α-helix | 4167-4181 | 15 | |
| β-strand | 4184-4188 | 5 | 17 |
| α-helix | 4190-4192 | 3 | |
| α-helix | 4194-4205 | 12 | |
| β-strand | 4214-4220 | 7 | 17 |
| α-helix | 4227-4232 | 6 | |
| β-strand | 4234-4238 | 5 | 17 |
| α-helix | 4244-4253 | 10 | |
| α-helix | 4257-4260 | 4 | |
| α-helix | 4266-4284 | 19 | |
| α-helix | 4285-4287 | 3 | |
| α-helix | 4300-4318 | 19 | |
| α-helix | 4326-4328 | 3 | |
| α-helix | 4331-4337 | 7 | |
| α-helix | 4338-4342 | 5 | |
| α-helix | 4344-4346 | 3 | |
| α-helix | 4350-4363 | 14 | |
| α-helix | 4366-4369 | 4 | |
| β-strand | 4374-4376 | 3 | 19 |
| α-helix | 4377-4379 | 3 | |
| β-strand | 4381-4382 | 2 | 19 |
| α-helix | 4389-4397 | 9 | |
| α-helix | 4405-4408 | 4 | |
| α-helix | 4412-4414 | 3 | |
| α-helix | 4416-4434 | 19 | |
| α-helix | 4453-4457 | 5 | |
| α-helix | 4463-4476 | 14 | |
| α-helix | 4477-4486 | 10 | |
| α-helix | 4490-4492 | 3 | |
| α-helix | 4494-4525 | 32 | |
| α-helix | 4532-4542 | 11 | |
| α-helix | 4561-4571 | 11 | |
| α-helix | 4574 | 1 | |
| α-helix | 4575-4579 | 5 | |
| α-helix | 4584-4586 | 3 | |
| β-strand | 4589-4590 | 2 | 20 |
| α-helix | 4597-4612 | 16 | |
| α-helix | 4616-4618 | 3 | |
| β-strand | 4619-4626 | 8 | 20 |
| β-strand | 4636-4640 | 5 | 20 |
| β-strand | 4647-4650 | 4 | 21 |
| β-strand | 4653-4656 | 4 | 21 |
| β-strand | 4667-4673 | 7 | 20 |
| α-helix | 4677-4684 | 8 | |
| β-strand | 4686-4691 | 6 | 22 |
| β-strand | 4699-4705 | 7 | 22 |
| β-strand | 4707 | 1 | 21 |
| α-helix | 4713-4718 | 6 | |
| β-strand | 4723-4724 | 2 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dynein heavy chain, cytoplasmic | A | protein | 3367 | Dictyostelium discoideum AX2 | P34036 |
>27PT_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
| ID | Name | Formula | Copies |
|---|---|---|---|
| AOV | ADP orthovanadate | C10 H17 N5 O14 P2 V | 1 |
| MG | Magnesium ion | Mg | 2 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
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:
MolViewer shows 27PT directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.