Tubulin:TM-3 DARPin complex. Determined by X-ray diffraction at 2.69 Å resolution. Released 24 Apr 2019.
Explore 6GVN in 3D Show helices and sheets RCSB PDB PDBe
6GVN contains 65 α-helices and 34 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 | 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 | 73-80 | 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 | 175-177 | 3 | |
| α-helix | 183-194 | 12 | |
| α-helix | 195-197 | 3 | |
| β-strand | 200-205 | 6 | 1 |
| α-helix | 206-215 | 10 | |
| α-helix | 224-244 | 21 | |
| α-helix | 252-259 | 8 | |
| α-helix | 268 | 1 | |
| β-strand | 269-273 | 5 | 3 |
| β-strand | 277 | 1 | 4 |
| α-helix | 285-287 | 3 | |
| α-helix | 288-293 | 6 | |
| α-helix | 294-296 | 3 | |
| α-helix | 298-300 | 3 | |
| β-strand | 301 | 1 | 3 |
| β-strand | 312-321 | 10 | 3 |
| α-helix | 325-337 | 13 | |
| α-helix | 342 | 1 | |
| β-strand | 343 | 1 | 3 |
| α-helix | 344 | 1 | |
| β-strand | 352-356 | 5 | 3 |
| α-helix | 359-360 | 2 | |
| 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 | 416-435 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 5 |
| α-helix | 10-28 | 19 | |
| β-strand | 30 | 1 | 6 |
| β-strand | 35 | 1 | 7 |
| β-strand | 36 | 1 | 6 |
| α-helix | 41-43 | 3 | |
| α-helix | 49-51 | 3 | |
| β-strand | 53-56 | 4 | 7 |
| β-strand | 60-63 | 4 | 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 | 103-108 | 6 | |
| α-helix | 110-127 | 18 | |
| β-strand | 132-140 | 9 | 5 |
| α-helix | 145-149 | 5 | |
| α-helix | 150-160 | 11 | |
| β-strand | 165-172 | 8 | 5 |
| 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 | 8 |
| α-helix | 288-295 | 8 | |
| α-helix | 298-300 | 3 | |
| β-strand | 301 | 1 | 8 |
| α-helix | 307-309 | 3 | |
| β-strand | 312-321 | 10 | 8 |
| α-helix | 325-338 | 14 | |
| α-helix | 340-342 | 3 | |
| β-strand | 343 | 1 | 8 |
| β-strand | 351-356 | 6 | 8 |
| α-helix | 359-360 | 2 | |
| β-strand | 373-381 | 9 | 8 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-400 | 16 | |
| α-helix | 405-409 | 5 | |
| α-helix | 415-437 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-24 | 11 | |
| α-helix | 27-35 | 9 | |
| α-helix | 50-56 | 7 | |
| α-helix | 60-68 | 9 | |
| α-helix | 83-90 | 8 | |
| α-helix | 93-101 | 9 | |
| α-helix | 116-122 | 7 | |
| α-helix | 126-134 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin alpha chain | A | protein | 451 | Ovis aries | D0VWZ0 (AlphaFold model) |
| Tubulin beta chain | B | protein | 445 | Ovis aries | D0VWY9 (AlphaFold model) |
| Tm-3 darpin | F | protein | 169 | synthetic construct |
>6GVN_1 Tubulin alpha chain (chains A) MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE AREDMAALEKDYEEVGVDSVEGEGEEEGEEY
>6GVN_2 Tubulin beta chain (chains B) MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYV PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVV EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMM AACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS EYQQYQDATADEQGEFEEEEGEDEA
>6GVN_3 TM-3 DARPIN (chains F) MRGSHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNATDASGLTPLHLAATYGHL EIVEVLLKHGADVNAIDIMGSTPLHLAALIGHLEIVEVLLKHGADVNAVDTWGDTPLRLA AIMGHLEIVEVLLKHGADVNAQDKFGKTAFDTSIDNGSEDLAEILQKLN
Water and common crystallization additives (GOL, MES, SO4) are not listed.
Insight into microtubule nucleation from tubulin-capping proteins. Campanacci, V., Urvoas, A., Cantos-Fernandes, S. et al. Proc Natl Acad Sci U S A (2019) 116:9859-9864. DOI 10.1073/pnas.1813559116 · PubMed
Other PDB entries of the same protein (UniProt D0VWZ0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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