Cryo-EM structure of the TBC-DE-Arl2-beta-tubulin complex with GTP. Determined by electron microscopy at 2.45 Å resolution. Released 22 Oct 2025.
Explore 9M1K in 3D Show helices and sheets RCSB PDB PDBe
9M1K contains 102 α-helices and 37 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-9 | 8 | 6 |
| α-helix | 11-25 | 15 | |
| β-strand | 30 | 1 | 7 |
| β-strand | 36 | 1 | 7 |
| α-helix | 47-49 | 3 | |
| β-strand | 51-53 | 3 | 8 |
| β-strand | 59-61 | 3 | 8 |
| β-strand | 63-66 | 4 | 6 |
| α-helix | 70-77 | 8 | |
| α-helix | 87-89 | 3 | |
| β-strand | 90-91 | 2 | 6 |
| α-helix | 101-102 | 2 | |
| α-helix | 103-107 | 5 | |
| α-helix | 109-126 | 18 | |
| β-strand | 129-136 | 8 | 6 |
| α-helix | 143-158 | 16 | |
| β-strand | 163-166 | 4 | 6 |
| β-strand | 169-170 | 2 | 9 |
| α-helix | 181-184 | 4 | |
| α-helix | 187-194 | 8 | |
| β-strand | 198-200 | 3 | 6 |
| β-strand | 202-203 | 2 | 9 |
| α-helix | 204-213 | 10 | |
| α-helix | 222-236 | 15 | |
| α-helix | 238-241 | 4 | |
| α-helix | 250-257 | 8 | |
| β-strand | 265-266 | 2 | 6 |
| β-strand | 267-268 | 2 | 10 |
| β-strand | 269 | 1 | 11 |
| α-helix | 286-293 | 8 | |
| α-helix | 296-298 | 3 | |
| β-strand | 299 | 1 | 11 |
| β-strand | 313-319 | 7 | 10 |
| α-helix | 323-333 | 11 | |
| β-strand | 349 | 1 | 10 |
| β-strand | 352-354 | 3 | 10 |
| α-helix | 357-358 | 2 | |
| β-strand | 363-369 | 7 | 10 |
| α-helix | 372-374 | 3 | |
| α-helix | 375-389 | 15 | |
| α-helix | 395-399 | 5 | |
| α-helix | 405-426 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-41 | 9 | |
| α-helix | 51-65 | 15 | |
| α-helix | 71-74 | 4 | |
| α-helix | 78-86 | 9 | |
| α-helix | 96-112 | 17 | |
| α-helix | 115-118 | 4 | |
| α-helix | 130-133 | 4 | |
| α-helix | 135-138 | 4 | |
| α-helix | 149-160 | 12 | |
| α-helix | 185-196 | 12 | |
| α-helix | 203-215 | 13 | |
| α-helix | 218-221 | 4 | |
| α-helix | 226-236 | 11 | |
| α-helix | 244-262 | 19 | |
| α-helix | 270-281 | 12 | |
| α-helix | 291-308 | 18 | |
| α-helix | 358-368 | 11 | |
| α-helix | 374-388 | 15 | |
| α-helix | 393-405 | 13 | |
| α-helix | 413-429 | 17 | |
| α-helix | 434-436 | 3 | |
| α-helix | 437-445 | 9 | |
| β-strand | 452-453 | 2 | 3 |
| β-strand | 458-459 | 2 | 3 |
| α-helix | 461-477 | 17 | |
| α-helix | 480-483 | 4 | |
| α-helix | 484-486 | 3 | |
| α-helix | 488-497 | 10 | |
| α-helix | 504-520 | 17 | |
| α-helix | 527-533 | 7 | |
| α-helix | 542-545 | 4 | |
| α-helix | 548-554 | 7 | |
| α-helix | 557-559 | 3 | |
| α-helix | 561-569 | 9 | |
| α-helix | 571-573 | 3 | |
| α-helix | 577-591 | 15 | |
| α-helix | 597-600 | 4 | |
| α-helix | 603-608 | 6 | |
| α-helix | 609-611 | 3 | |
| α-helix | 615-638 | 24 | |
| α-helix | 643-645 | 3 | |
| α-helix | 649-655 | 7 | |
| α-helix | 658-664 | 7 | |
| α-helix | 670-689 | 20 | |
| α-helix | 698-712 | 15 | |
| α-helix | 722-739 | 18 | |
| α-helix | 750-762 | 13 | |
| α-helix | 763-765 | 3 | |
| α-helix | 769-780 | 12 | |
| α-helix | 791-801 | 11 | |
| α-helix | 812-829 | 18 | |
| β-strand | 831 | 1 | 4 |
| β-strand | 840 | 1 | 4 |
| α-helix | 845-856 | 12 | |
| α-helix | 868-886 | 19 | |
| α-helix | 891-893 | 3 | |
| α-helix | 896-910 | 15 | |
| α-helix | 915-929 | 15 | |
| α-helix | 935-936 | 2 | |
| α-helix | 942-948 | 7 | |
| α-helix | 962-964 | 3 | |
| α-helix | 966-969 | 4 | |
| α-helix | 970-974 | 5 | |
| α-helix | 977-979 | 3 | |
| α-helix | 980-990 | 11 | |
| α-helix | 995-1010 | 16 | |
| α-helix | 1016-1031 | 16 | |
| α-helix | 1037-1053 | 17 | |
| α-helix | 1058-1060 | 3 | |
| α-helix | 1066-1079 | 14 | |
| α-helix | 1085-1097 | 13 | |
| α-helix | 1098-1100 | 3 | |
| α-helix | 1104-1116 | 13 | |
| α-helix | 1122-1138 | 17 | |
| α-helix | 1145-1156 | 12 | |
| α-helix | 1164-1178 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 446-451 | 6 | 1 |
| β-strand | 461-465 | 5 | 1 |
| β-strand | 470 | 1 | 2 |
| α-helix | 471-482 | 12 | |
| β-strand | 490-494 | 5 | 1 |
| β-strand | 503-504 | 2 | 1 |
| β-strand | 511 | 1 | 2 |
| β-strand | 522-526 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| β-strand | 16-22 | 7 | 5 |
| α-helix | 29-37 | 9 | |
| β-strand | 50-57 | 8 | 5 |
| β-strand | 60-67 | 8 | 5 |
| α-helix | 71-74 | 4 | |
| α-helix | 77-80 | 4 | |
| β-strand | 86-92 | 7 | 5 |
| α-helix | 99-111 | 13 | |
| β-strand | 119-125 | 7 | 5 |
| α-helix | 135-141 | 7 | |
| β-strand | 151 | 1 | 5 |
| α-helix | 165-179 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin-specific chaperone E | E | protein | 527 | Homo sapiens | Q15813 (AlphaFold model) |
| Tubulin-specific chaperone D | D | protein | 1192 | Homo sapiens | Q9BTW9 (AlphaFold model) |
| ADP-ribosylation factor-like protein 2 | G | protein | 184 | Homo sapiens | P36404 (AlphaFold model) |
| Tubulin beta chain | b | protein | 444 | Sus scrofa | Q767L7 (AlphaFold model) |
>9M1K_1 Tubulin-specific chaperone E (chains E) MSDTLTADVIGRRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFK CRHPTGGSFIRPNKVNFGTDFLTAIKNRYVLEDGPEEDRKEQIVTIGNKPVETIGFDSIM KQQSQLSKLQEVSLRNCAVSCAGEKGGVAEACPNIRKVDLSKNLLSSWDEVIHIADQLRH LEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITWAEVLRCVAGCPGLEELYLESNN IFISERPTDVLQTVKLLDLSSNQLIDENQLYLIAHLPRLEQLILSDTGISSLHFPDAGIG CKTSMFPSLKYLVVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEDKEAETARLLIIA SIGQLKTLNKCEILPEERRRAELDYRKAFGNEWKQAGGHKDPEKNRLSEEFLTAHPRYQF LCLKYGAPEDWELKTQQPLMLKNQLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSR LLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCLLVRW
>9M1K_2 Tubulin-specific chaperone D (chains D) MALSDEPAAGGPEEEAEDETLAFGAALEAFGESAETRALLGRLREVHGGGAEREVALERF RVIMDKYQEQPHLLDPHLEWMMNLLLDIVQDQTSPASLVHLAFKFLYIITKVRGYKTFLR LFPHEVADVEPVLDLVTIQNPKDHEAWETRYMLLLWLSVTCLIPFDFSRLDGNLLTQPGQ ARMSIMDRILQIAESYLIVSDKARDAAAVLVSRFITRPDVKQSKMAEFLDWSLCNLARSS FQTMQGVITMDGTLQALAQIFKHGKREDCLPYAATVLRCLDGCRLPESNQTLLRKLGVKL VQRLGLTFLKPKVAAWRYQRGCRSLAANLQLLTQGQSEQKPLILTEDDDEDDDVPEGVER VIEQLLVGLKDKDTVVRWSAAKGIGRMAGRLPRALADDVVGSVLDCFSFQETDKAWHGGC LALAELGRRGLLLPSRLVDVVAVILKALTYDEKRGACSVGTNVRDAACYVCWAFARAYEP QELKPFVTAISSALVIAAVFDRDINCRRAASAAFQENVGRQGTFPHGIDILTTADYFAVG NRSNCFLVISVFIAGFPEYTQPMIDHLVTMKISHWDGVIRELAARALHNLAQQAPEFSAT QVFPRLLSMTLSPDLHMRHGSILACAEVAYALYKLAAQENRPVTDHLDEQAVQGLKQIHQ QLYDRQLYRGLGGQLMRQAVCVLIEKLSLSKMPFRGDTVIDGWQWLINDTLRHLHLISSH SRQQMKDAAVSALAALCSEYYMKEPGEADPAIQEELITQYLAELRNPEEMTRCGFSLALG ALPGFLLKGRLQQVLTGLRAVTHTSPEDVSFAESRRDGLKAIARICQTVGVKAGAPDEAV CGENVSQIYCALLGCMDDYTTDSRGDVGTWVRKAAMTSLMDLTLLLARSQPELIEAHTCE RIMCCVAQQASEKIDRFRAHAASVFLTLLHFDSPPIPHVPHRGELEKLFPRSDVASVNWS APSQAFPRITQLLGLPTYRYHVLLGLVVSLGGLTESTIRHSTQSLFEYMKGIQSDPQALG SFSGTLLQIFEDNLLNERVSVPLLKTLDHVLTHGCFDIFTTEEDHPFAVKLLALCKKEIK NSKDIQKLLSGIAVFCEMVQFPGDVRRQALLQLCLLLCHRFPLIRKTTASQVYETLLTYS DVVGADVLDEVVTVLSDTAWDAELAVVREQRNRLCDLLGVPRPQLVPQPGAC
>9M1K_3 ADP-ribosylation factor-like protein 2 (chains G) MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGF KLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATL LIFANKQDLPGALSSNAIREVLELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRI FTAD
>9M1K_4 Tubulin beta chain (chains b) MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYV PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMM AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS EYQQYQDATAEEEEDFGEEAEEEA
Structural dissection of alpha beta-tubulin heterodimer assembly and disassembly by human tubulin-specific chaperones. Seong, Y., Kim, H., Byun, K. et al. Science (2025) 390:eady2708-eady2708. DOI 10.1126/science.ady2708 · PubMed
Other PDB entries of the same protein (UniProt Q15813 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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