Cryo-EM structure of the TBC-D-Arl2-beta-tubulin complex. Determined by electron microscopy at 2.48 Å resolution. Released 22 Oct 2025.
Explore 9M1I in 3D Show helices and sheets RCSB PDB PDBe
9M1I contains 99 α-helices and 44 β-strands across 3 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 | 3-9 | 7 | 9 |
| α-helix | 12-24 | 13 | |
| β-strand | 30 | 1 | 10 |
| β-strand | 36 | 1 | 10 |
| α-helix | 44-49 | 6 | |
| β-strand | 53 | 1 | 11 |
| β-strand | 59 | 1 | 11 |
| β-strand | 63-67 | 5 | 9 |
| α-helix | 71-76 | 6 | |
| β-strand | 90-92 | 3 | 9 |
| α-helix | 101-102 | 2 | |
| α-helix | 103-107 | 5 | |
| α-helix | 109-126 | 18 | |
| β-strand | 130-136 | 7 | 9 |
| α-helix | 143-158 | 16 | |
| β-strand | 163-167 | 5 | 9 |
| β-strand | 169-170 | 2 | 12 |
| α-helix | 181-192 | 12 | |
| β-strand | 198-200 | 3 | 9 |
| β-strand | 202-203 | 2 | 12 |
| α-helix | 204-209 | 6 | |
| α-helix | 210-214 | 5 | |
| α-helix | 222-236 | 15 | |
| α-helix | 250-257 | 8 | |
| β-strand | 265-266 | 2 | 9 |
| β-strand | 267-271 | 5 | 13 |
| α-helix | 286-292 | 7 | |
| α-helix | 296-298 | 3 | |
| β-strand | 299 | 1 | 13 |
| β-strand | 310 | 1 | 14 |
| β-strand | 314 | 1 | 15 |
| β-strand | 315-318 | 4 | 13 |
| α-helix | 323-333 | 11 | |
| β-strand | 350 | 1 | 15 |
| β-strand | 364-369 | 6 | 13 |
| β-strand | 371 | 1 | 14 |
| α-helix | 372-374 | 3 | |
| α-helix | 375-389 | 15 | |
| α-helix | 396-399 | 4 | |
| α-helix | 405-424 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 21-23 | 3 | 1 |
| α-helix | 33-40 | 8 | |
| α-helix | 53-64 | 12 | |
| α-helix | 65-67 | 3 | |
| α-helix | 71-74 | 4 | |
| α-helix | 80-89 | 10 | |
| α-helix | 96-112 | 17 | |
| α-helix | 118-120 | 3 | |
| α-helix | 126-128 | 3 | |
| α-helix | 130-138 | 9 | |
| α-helix | 144-146 | 3 | |
| α-helix | 147-160 | 14 | |
| α-helix | 185-195 | 11 | |
| α-helix | 203-215 | 13 | |
| α-helix | 225-237 | 13 | |
| α-helix | 244-262 | 19 | |
| α-helix | 266-269 | 4 | |
| α-helix | 273-281 | 9 | |
| α-helix | 291-308 | 18 | |
| α-helix | 356-368 | 13 | |
| α-helix | 376-388 | 13 | |
| α-helix | 393-405 | 13 | |
| α-helix | 413-428 | 16 | |
| α-helix | 434-448 | 15 | |
| β-strand | 452-454 | 3 | 2 |
| β-strand | 457-459 | 3 | 2 |
| α-helix | 461-477 | 17 | |
| α-helix | 481-483 | 3 | |
| α-helix | 484-497 | 14 | |
| α-helix | 504-521 | 18 | |
| α-helix | 528-533 | 6 | |
| α-helix | 536-539 | 4 | |
| α-helix | 542-544 | 3 | |
| α-helix | 545-549 | 5 | |
| α-helix | 550-554 | 5 | |
| α-helix | 561-566 | 6 | |
| α-helix | 567-571 | 5 | |
| α-helix | 577-590 | 14 | |
| α-helix | 595-597 | 3 | |
| α-helix | 598-602 | 5 | |
| α-helix | 603-609 | 7 | |
| α-helix | 615-637 | 23 | |
| α-helix | 649-656 | 8 | |
| α-helix | 659-664 | 6 | |
| α-helix | 673-688 | 16 | |
| α-helix | 698-712 | 15 | |
| α-helix | 719-721 | 3 | |
| α-helix | 723-740 | 18 | |
| α-helix | 750-760 | 11 | |
| α-helix | 769-780 | 12 | |
| α-helix | 792-802 | 11 | |
| α-helix | 812-829 | 18 | |
| β-strand | 831 | 1 | 3 |
| β-strand | 840 | 1 | 3 |
| α-helix | 845-853 | 9 | |
| β-strand | 861-863 | 3 | 4 |
| β-strand | 865-866 | 2 | 4 |
| α-helix | 869-888 | 20 | |
| α-helix | 891-893 | 3 | |
| α-helix | 896-908 | 13 | |
| α-helix | 909-911 | 3 | |
| α-helix | 915-929 | 15 | |
| β-strand | 932 | 1 | 5 |
| β-strand | 935 | 1 | 5 |
| α-helix | 936 | 1 | |
| α-helix | 942-948 | 7 | |
| α-helix | 951-956 | 6 | |
| α-helix | 962-969 | 8 | |
| α-helix | 970-974 | 5 | |
| α-helix | 977-979 | 3 | |
| α-helix | 981-990 | 10 | |
| α-helix | 995-1008 | 14 | |
| α-helix | 1009-1011 | 3 | |
| α-helix | 1016-1032 | 17 | |
| α-helix | 1040-1051 | 12 | |
| α-helix | 1066-1076 | 11 | |
| α-helix | 1085-1097 | 13 | |
| α-helix | 1098-1100 | 3 | |
| α-helix | 1104-1115 | 12 | |
| α-helix | 1116-1118 | 3 | |
| α-helix | 1122-1138 | 17 | |
| α-helix | 1145-1156 | 12 | |
| α-helix | 1164-1178 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-10 | 7 | |
| α-helix | 11-15 | 5 | |
| β-strand | 16 | 1 | 6 |
| β-strand | 19-21 | 3 | 1 |
| β-strand | 23 | 1 | 1 |
| α-helix | 27-36 | 10 | |
| β-strand | 50-54 | 5 | 1 |
| β-strand | 57 | 1 | 7 |
| β-strand | 60 | 1 | 7 |
| β-strand | 61 | 1 | 6 |
| β-strand | 63-67 | 5 | 1 |
| β-strand | 78 | 1 | 8 |
| β-strand | 83 | 1 | 8 |
| β-strand | 86-87 | 2 | 1 |
| β-strand | 90-92 | 3 | 1 |
| α-helix | 99-109 | 11 | |
| β-strand | 119-125 | 7 | 1 |
| α-helix | 135-142 | 8 | |
| β-strand | 152-155 | 4 | 1 |
| α-helix | 166-177 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 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) |
>9M1I_1 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
>9M1I_2 ADP-ribosylation factor-like protein 2 (chains G) MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGF KLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATL LIFANKQDLPGALSSNAIREVLELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRI FTAD
>9M1I_3 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 Q9BTW9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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