Human doublecortin N-DC repeat plus linker, and tubulin (2XRP) docked into an 8A cryo-EM map of doublecortin-stabilised microtubules reconstructed in absence of kinesin. Determined by electron microscopy at 8.3 Å resolution. Released 26 Sept 2012.
Explore 4ATU in 3D Show helices and sheets RCSB PDB PDBe
4ATU contains 167 α-helices and 129 β-strands across 9 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 | 1 | 1 |
| β-strand | 6-9 | 4 | 1 |
| α-helix | 12-26 | 15 | |
| β-strand | 30 | 1 | 2 |
| β-strand | 36 | 1 | 2 |
| α-helix | 49-52 | 4 | |
| β-strand | 55 | 1 | 3 |
| β-strand | 61 | 1 | 3 |
| β-strand | 65-69 | 5 | 1 |
| α-helix | 72-78 | 7 | |
| α-helix | 83-85 | 3 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 1 |
| α-helix | 105-109 | 5 | |
| α-helix | 111-126 | 16 | |
| β-strand | 134-139 | 6 | 1 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-160 | 12 | |
| β-strand | 165-170 | 6 | 1 |
| α-helix | 184-194 | 11 | |
| β-strand | 200-202 | 3 | 1 |
| α-helix | 206-214 | 9 | |
| α-helix | 224-242 | 19 | |
| β-strand | 248 | 1 | 4 |
| α-helix | 252-259 | 8 | |
| β-strand | 267-268 | 2 | 1 |
| β-strand | 269-271 | 3 | 4 |
| α-helix | 289-295 | 7 | |
| α-helix | 307-309 | 3 | |
| β-strand | 312-320 | 9 | 4 |
| α-helix | 325-338 | 14 | |
| β-strand | 351-356 | 6 | 4 |
| β-strand | 375-381 | 7 | 4 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 403-405 | 3 | |
| α-helix | 406-409 | 4 | |
| α-helix | 415-436 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 5 |
| α-helix | 10-26 | 17 | |
| β-strand | 65-69 | 5 | 5 |
| α-helix | 73-78 | 6 | |
| β-strand | 92-94 | 3 | 5 |
| α-helix | 103-107 | 5 | |
| α-helix | 109-128 | 20 | |
| β-strand | 134-139 | 6 | 5 |
| α-helix | 144-149 | 6 | |
| α-helix | 150-160 | 11 | |
| β-strand | 165 | 1 | 5 |
| β-strand | 167-170 | 4 | 5 |
| α-helix | 184-194 | 11 | |
| β-strand | 200-203 | 4 | 5 |
| α-helix | 206-215 | 10 | |
| α-helix | 224-242 | 19 | |
| α-helix | 252-259 | 8 | |
| β-strand | 269-271 | 3 | 5 |
| β-strand | 277 | 1 | 6 |
| α-helix | 284-287 | 4 | |
| α-helix | 288-294 | 7 | |
| α-helix | 298-300 | 3 | |
| β-strand | 312-321 | 10 | 5 |
| α-helix | 325-336 | 12 | |
| β-strand | 343 | 1 | 5 |
| β-strand | 351-355 | 5 | 5 |
| β-strand | 368 | 1 | 6 |
| β-strand | 373-381 | 9 | 5 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 403-405 | 3 | |
| α-helix | 406-409 | 4 | |
| α-helix | 415-429 | 15 | |
| α-helix | 431-434 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 53-59 | 7 | 25 |
| β-strand | 68-72 | 5 | 25 |
| α-helix | 80-90 | 11 | |
| β-strand | 103-106 | 4 | 25 |
| β-strand | 112-113 | 2 | 25 |
| α-helix | 116-118 | 3 | |
| α-helix | 119-120 | 2 | |
| β-strand | 123-128 | 6 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin beta-2B chain | A, C, E, G | protein | 445 | BOS TAURUS | Q6B856 (AlphaFold model) |
| Tubulin alpha-1D chain | B, D, F, H | protein | 452 | BOS TAURUS | Q2HJ86 (AlphaFold model) |
| Neuronal migration protein doublecortin | I | protein | 373 | HOMO SAPIENS | O43602 (AlphaFold model) |
>4ATU_1 TUBULIN BETA-2B CHAIN (chains A, C, E, G) MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS EYQQYQDATADEQGEFEEEEGEDEA
>4ATU_2 TUBULIN ALPHA-1D CHAIN (chains B, D, F, H) MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRGHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE AREDMAALEKDYEEVGVDSVEGEGEEEEGEEY
>4ATU_3 NEURONAL MIGRATION PROTEIN DOUBLECORTIN (chains I) GAMDYKDDDDKICRELDFGHFDERDKTSRNMRGSRMNGLPSPTHSAHCSFYRTRTLQALS NEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRYIYTI DGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNVNPNWSVNVKTSANMKAPQSLASSNS AQARENKDFVRPKLVTIIRSGVKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLETGVVKK LYTLDGKQVTCLHDFFGDDDVFIACGPEKFRYAQDDFSLDENECRVMKGNPSATAGPKAS PTPQKTSAKSPGPMRRSKSPADSANGTSSSQLSTPKSKQSPISTPTSPGSLRKHKDLYLP LSLDDSDSLGDSM
| ID | Name | Formula | Copies |
|---|---|---|---|
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 4 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 4 |
Molecular Basis for Specific Regulation of Neuronal Kinesin- 3 Motors by Doublecortin Family Proteins. Liu, J.S., Schubert, C.R., Fu, X. et al. Mol Cell (2012) 47:707. DOI 10.1016/J.MOLCEL.2012.06.025 · PubMed
Other PDB entries of the same protein (UniProt Q6B856 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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