9H32: T2R-TTL-PROTAC3 complex
T2R-TTL-PROTAC3 complex. Determined by X-ray diffraction at 2.31 Å resolution. Released 29 Oct 2025.
- Method
- X-ray diffraction
- Resolution
- 2.31 Å
- Organisms
- Bos taurus, Rattus norvegicus, Gallus gallus
- Chains
- 6
- Atoms
- 17,883
- Mol. weight
- 265.64 kDa
- Ligands
- GTP, MG, CA, ACP
- Released
- 29 Oct 2025
Explore 9H32 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9H32 contains 128 α-helices and 93 β-strands across 6 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.
Chain A: 26 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-9 | 6 | 1 |
| α-helix | 10-28 | 19 | |
| α-helix | 48-51 | 4 | |
| β-strand | 53-55 | 3 | 2 |
| β-strand | 61-63 | 3 | 2 |
| β-strand | 65-69 | 5 | 1 |
| α-helix | 72-79 | 8 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 1 |
| α-helix | 103-104 | 2 | |
| α-helix | 105-109 | 5 | |
| α-helix | 111-113 | 3 | |
| α-helix | 115-127 | 13 | |
| β-strand | 134-140 | 7 | 1 |
| α-helix | 144 | 1 | |
| α-helix | 145-149 | 5 | |
| α-helix | 150-160 | 11 | |
| β-strand | 165-172 | 8 | 1 |
| α-helix | 183-195 | 13 | |
| β-strand | 200-205 | 6 | 1 |
| α-helix | 206-216 | 11 | |
| α-helix | 224-243 | 20 | |
| α-helix | 252-259 | 8 | |
| β-strand | 269-273 | 5 | 3 |
| β-strand | 277 | 1 | 4 |
| α-helix | 284-286 | 3 | |
| α-helix | 288-294 | 7 | |
| α-helix | 298-300 | 3 | |
| β-strand | 301 | 1 | 3 |
| α-helix | 307-309 | 3 | |
| β-strand | 312-321 | 10 | 3 |
| α-helix | 325-336 | 12 | |
| β-strand | 343 | 1 | 3 |
| β-strand | 349-356 | 8 | 3 |
| α-helix | 359-361 | 3 | |
| β-strand | 368 | 1 | 4 |
| α-helix | 369-370 | 2 | |
| β-strand | 373-381 | 9 | 3 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 405-409 | 5 | |
| α-helix | 416-436 | 21 | |
Chain B: 29 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 5 |
| α-helix | 10-27 | 18 | |
| β-strand | 30 | 1 | 6 |
| β-strand | 36 | 1 | 6 |
| α-helix | 42-47 | 4 | |
| α-helix | 49-51 | 3 | |
| β-strand | 53-55 | 3 | 7 |
| α-helix | 57-59 | 3 | |
| β-strand | 61-63 | 3 | 7 |
| β-strand | 65-69 | 5 | 5 |
| α-helix | 73-80 | 8 | |
| α-helix | 84-86 | 3 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 5 |
| α-helix | 103-107 | 5 | |
| α-helix | 110-127 | 18 | |
| β-strand | 131-140 | 10 | 5 |
| α-helix | 145-149 | 5 | |
| α-helix | 150-160 | 11 | |
| β-strand | 165-172 | 8 | 5 |
| α-helix | 173 | 1 | |
| β-strand | 174 | 1 | 8 |
| β-strand | 177 | 1 | 8 |
| α-helix | 183-197 | 15 | |
| β-strand | 200-205 | 6 | 5 |
| α-helix | 206-211 | 6 | |
| α-helix | 212-216 | 5 | |
| α-helix | 224-238 | 15 | |
| α-helix | 240-243 | 4 | |
| α-helix | 252-259 | 8 | |
| β-strand | 267-268 | 2 | 5 |
| β-strand | 269-273 | 5 | 9 |
| α-helix | 285-287 | 3 | |
| α-helix | 288-296 | 9 | |
| α-helix | 298-300 | 3 | |
| β-strand | 301 | 1 | 9 |
| α-helix | 307-309 | 3 | |
| β-strand | 312-321 | 10 | 9 |
| α-helix | 325-338 | 14 | |
| α-helix | 340-342 | 3 | |
| β-strand | 343 | 1 | 9 |
| β-strand | 351-356 | 6 | 9 |
| α-helix | 359-360 | 2 | |
| β-strand | 373-381 | 9 | 9 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 406-409 | 4 | |
| α-helix | 415-435 | 21 | |
Chain C: 29 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-9 | 6 | 10 |
| α-helix | 10-28 | 19 | |
| β-strand | 35 | 1 | 11 |
| α-helix | 48-51 | 4 | |
| β-strand | 53-55 | 3 | 12 |
| β-strand | 60 | 1 | 11 |
| β-strand | 61-63 | 3 | 12 |
| β-strand | 65-69 | 5 | 10 |
| α-helix | 73-80 | 8 | |
| α-helix | 84-86 | 3 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 10 |
| α-helix | 103-104 | 2 | |
| α-helix | 105-109 | 5 | |
| α-helix | 111-113 | 3 | |
| α-helix | 115-127 | 13 | |
| β-strand | 134-140 | 7 | 10 |
| α-helix | 144 | 1 | |
| α-helix | 145-149 | 5 | |
| α-helix | 150-161 | 12 | |
| β-strand | 165-172 | 8 | 10 |
| α-helix | 183-195 | 13 | |
| β-strand | 200-205 | 6 | 10 |
| α-helix | 206-217 | 12 | |
| α-helix | 224-243 | 20 | |
| α-helix | 252-259 | 8 | |
| α-helix | 268 | 1 | |
| β-strand | 269-273 | 5 | 13 |
| β-strand | 277 | 1 | 14 |
| α-helix | 278-281 | 4 | |
| α-helix | 288-294 | 7 | |
| α-helix | 298-300 | 3 | |
| β-strand | 301 | 1 | 13 |
| α-helix | 307-309 | 3 | |
| β-strand | 312-321 | 10 | 13 |
| α-helix | 325-336 | 12 | |
| β-strand | 343 | 1 | 13 |
| α-helix | 350-351 | 2 | |
| β-strand | 352-356 | 5 | 13 |
| α-helix | 359-360 | 2 | |
| β-strand | 368 | 1 | 14 |
| β-strand | 373-381 | 9 | 13 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-400 | 16 | |
| α-helix | 405-409 | 5 | |
| α-helix | 415-435 | 21 | |
| α-helix | 438-439 | 2 | |
Chain D: 27 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-9 | 7 | 15 |
| α-helix | 10-27 | 18 | |
| β-strand | 30 | 1 | 16 |
| β-strand | 36 | 1 | 16 |
| α-helix | 41-45 | 3 | |
| α-helix | 49-51 | 3 | |
| β-strand | 53-56 | 4 | 17 |
| β-strand | 60-63 | 4 | 17 |
| β-strand | 65-69 | 5 | 15 |
| α-helix | 72-80 | 9 | |
| α-helix | 84-86 | 3 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 15 |
| α-helix | 103-107 | 5 | |
| α-helix | 110-127 | 18 | |
| β-strand | 132-140 | 9 | 15 |
| α-helix | 145-149 | 5 | |
| α-helix | 150-160 | 11 | |
| β-strand | 165-172 | 8 | 15 |
| α-helix | 173 | 1 | |
| α-helix | 183-197 | 15 | |
| β-strand | 200-205 | 6 | 15 |
| α-helix | 206-211 | 6 | |
| α-helix | 212-216 | 5 | |
| α-helix | 224-238 | 15 | |
| α-helix | 240-243 | 4 | |
| α-helix | 252-259 | 8 | |
| β-strand | 267-268 | 2 | 15 |
| β-strand | 269-273 | 5 | 18 |
| α-helix | 288-295 | 8 | |
| α-helix | 298-300 | 3 | |
| β-strand | 301 | 1 | 18 |
| α-helix | 307-309 | 3 | |
| β-strand | 312-321 | 10 | 18 |
| α-helix | 325-338 | 14 | |
| α-helix | 340-342 | 3 | |
| β-strand | 343 | 1 | 18 |
| β-strand | 351-356 | 6 | 18 |
| α-helix | 359-360 | 2 | |
| β-strand | 373-381 | 9 | 18 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 406-409 | 4 | |
| α-helix | 415-437 | 23 | |
Chain E: 1 helix, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-13 | 7 | 3 |
| β-strand | 17-25 | 9 | 3 |
| α-helix | 47-140 | 94 | |
Chain F: 16 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-6 | 5 | 19 |
| α-helix | 12-23 | 12 | |
| β-strand | 27-29 | 3 | 19 |
| β-strand | 39-41 | 3 | 19 |
| α-helix | 49-51 | 3 | |
| β-strand | 61-62 | 2 | 19 |
| α-helix | 68-70 | 3 | |
| α-helix | 74-83 | 10 | |
| β-strand | 97-100 | 4 | 20 |
| α-helix | 128-140 | 13 | |
| β-strand | 147-150 | 4 | 20 |
| β-strand | 161-163 | 3 | 20 |
| α-helix | 166-174 | 9 | |
| β-strand | 180-184 | 5 | 20 |
| β-strand | 189 | 1 | 21 |
| β-strand | 192 | 1 | 22 |
| β-strand | 197 | 1 | 22 |
| β-strand | 201-207 | 7 | 23 |
| β-strand | 213-216 | 4 | 23 |
| β-strand | 220-222 | 3 | 23 |
| β-strand | 227 | 1 | 22 |
| α-helix | 243-249 | 7 | |
| α-helix | 258-260 | 3 | |
| β-strand | 261-263 | 3 | 23 |
| α-helix | 264-270 | 7 | |
| α-helix | 271-275 | 5 | |
| α-helix | 279 | 1 | |
| α-helix | 280-284 | 5 | |
| α-helix | 285-302 | 18 | |
| β-strand | 310-311 | 2 | 19 |
| β-strand | 313-321 | 9 | 23 |
| β-strand | 322 | 1 | 21 |
| β-strand | 327-333 | 7 | 23 |
| α-helix | 340-342 | 3 | |
| α-helix | 343-349 | 7 | |
| α-helix | 350-355 | 6 | |
| β-strand | 375-377 | 3 | 23 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Tubulin alpha-1B chain | A, C | protein | 451 | Bos taurus | P81947 (AlphaFold model) |
| Tubulin beta-2B chain | B, D | protein | 445 | Bos taurus | Q6B856 (AlphaFold model) |
| Stathmin-4 | E | protein | 143 | Rattus norvegicus | P63043 (AlphaFold model) |
| Tubulin--tyrosine ligase | F | protein | 384 | Gallus gallus | A0A8V0Z8P0 (AlphaFold model) |
Sequence of entity 1 (A, C), FASTA
>9H32_1 Tubulin alpha-1B chain (chains A, C)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Sequence of entity 2 (B, D), FASTA
>9H32_2 Tubulin beta-2B chain (chains B, D)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMM
AACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEEGEDEA
Sequence of entity 3 (E), FASTA
>9H32_3 Stathmin-4 (chains E)
MADMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRK
YQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLER
LQEKDKHAEEVRKNKELKEEASR
Sequence of entity 4 (F), FASTA
>9H32_4 Tubulin--tyrosine ligase (chains F)
MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQ
LVNYYRGADKLCRKASLVKLIKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLI
NNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGILISSEASELLDFIDEQGQVH
VIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEP
AISTKHLHYQSFQLFGFDFMVDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFP
LADTGQKTSQPTSIFIKLHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 2 |
| MG | Magnesium ion | Mg | 5 |
| CA | Calcium ion | Ca | 4 |
| ACP | Phosphomethylphosphonic acid adenylate ester | C11 H18 N5 O12 P3 | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
| A1ISD | (1S,2R,3S,5S,6S,16E,20R,21S)-11-chloro-21-hydroxy-12,20-dimethoxy-2,5,9,16-tetr… | C56 H65 Cl N8 O13 | 1 |
Water and common crystallization additives (MES) are not listed.
Primary citation
Effective Tubulin Degradation by Rationally Designed Proteolysis Targeting Chimeras. Maiocchi, A., Abel, A.C., Basellini, M. et al. bioRxiv (2025). DOI 10.1101/2025.05.22.655572
Other PDB entries of the same protein (UniProt P81947 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6S8K 1.52 Å, Structure, Thermodynamics, and Kinetics of Plinabulin Binding to two Tubulin Isotypes
- 8QL2 1.7 Å, Ultrafast structural transitions in an azobenzene photoswitch at near-atomic resolution:…
- 6ZWB 1.75 Å, Z-SBTub3 photoswitch bound to tubulin-DARPin D1 complex
- 4I4T 1.8 Å, Crystal structure of tubulin-RB3-TTL-Zampanolide complex
- 5IYZ 1.8 Å, Tubulin-MMAE complex
- 5NQU 1.8 Å, Tubulin Darpin cryo structure
- 7YZ3 1.8 Å, Molecular snapshots of drug release from tubulin: Apo state
- 8QEA 1.8 Å, Ultrafast structural transitions in an azobenzene photoswitch at near-atomic resolution:…
- 8QL3 1.8 Å, Ultrafast structural transitions in an azobenzene photoswitch at near-atomic resolution:…
- 8QL4 1.8 Å, Ultrafast structural transitions in an azobenzene photoswitch at near-atomic resolution:…
- 8QL5 1.8 Å, Ultrafast structural transitions in an azobenzene photoswitch at near-atomic resolution:…
- 8QL6 1.8 Å, Ultrafast structural transitions in an azobenzene photoswitch at near-atomic resolution:…
Browse structure collections
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