bovine sperm endpiece singlet microtubules (one tubulin dimer and associated microtubule inner proteins). Determined by electron microscopy at 3.5 Å resolution. Released 5 Jul 2023.
Explore 8OU0 in 3D Show helices and sheets RCSB PDB PDBe
8OU0 contains 53 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 | 3-9 | 7 | 5 |
| α-helix | 10-28 | 19 | |
| β-strand | 35 | 1 | 6 |
| α-helix | 49-51 | 3 | |
| β-strand | 53 | 1 | 7 |
| β-strand | 60 | 1 | 6 |
| β-strand | 63 | 1 | 7 |
| β-strand | 65-68 | 4 | 5 |
| α-helix | 73-80 | 8 | |
| β-strand | 92-93 | 2 | 5 |
| α-helix | 103-104 | 2 | |
| α-helix | 105-109 | 5 | |
| α-helix | 111-113 | 3 | |
| α-helix | 115-128 | 14 | |
| β-strand | 132-140 | 9 | 5 |
| α-helix | 144-160 | 17 | |
| β-strand | 165-171 | 7 | 5 |
| α-helix | 172-174 | 3 | |
| α-helix | 183-194 | 12 | |
| β-strand | 200-204 | 5 | 5 |
| α-helix | 206-212 | 7 | |
| α-helix | 213-217 | 5 | |
| α-helix | 224-243 | 20 | |
| β-strand | 248 | 1 | 8 |
| α-helix | 253-259 | 7 | |
| β-strand | 262 | 1 | 9 |
| β-strand | 265 | 1 | 9 |
| β-strand | 269-273 | 5 | 8 |
| α-helix | 278-282 | 5 | |
| α-helix | 288-294 | 7 | |
| α-helix | 298-300 | 3 | |
| α-helix | 307-309 | 3 | |
| β-strand | 312-321 | 10 | 8 |
| α-helix | 325-337 | 13 | |
| β-strand | 343 | 1 | 8 |
| β-strand | 351-356 | 6 | 8 |
| β-strand | 373-381 | 9 | 8 |
| α-helix | 384-400 | 17 | |
| α-helix | 405-411 | 7 | |
| α-helix | 415-436 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 1 |
| α-helix | 10-27 | 18 | |
| β-strand | 30 | 1 | 2 |
| β-strand | 35 | 1 | 3 |
| β-strand | 36 | 1 | 2 |
| β-strand | 53-56 | 4 | 3 |
| β-strand | 60-63 | 4 | 3 |
| β-strand | 65-69 | 5 | 1 |
| α-helix | 72-80 | 9 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 1 |
| α-helix | 103-104 | 2 | |
| α-helix | 105-109 | 5 | |
| α-helix | 111-128 | 18 | |
| β-strand | 132-140 | 9 | 1 |
| α-helix | 145-160 | 16 | |
| β-strand | 165-171 | 7 | 1 |
| α-helix | 183-197 | 15 | |
| β-strand | 200-204 | 5 | 1 |
| α-helix | 207-215 | 9 | |
| α-helix | 224-239 | 16 | |
| α-helix | 240-242 | 3 | |
| β-strand | 248 | 1 | 4 |
| α-helix | 252-259 | 8 | |
| β-strand | 267-268 | 2 | 1 |
| β-strand | 269-273 | 5 | 4 |
| α-helix | 288-295 | 8 | |
| β-strand | 301 | 1 | 4 |
| α-helix | 307-309 | 3 | |
| β-strand | 312-320 | 9 | 4 |
| α-helix | 325-338 | 14 | |
| α-helix | 340-342 | 3 | |
| β-strand | 343 | 1 | 4 |
| β-strand | 351-355 | 5 | 4 |
| α-helix | 359-360 | 2 | |
| β-strand | 374-381 | 8 | 4 |
| α-helix | 384-400 | 17 | |
| α-helix | 406-409 | 4 | |
| α-helix | 415-434 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-21 | 16 | |
| α-helix | 23-36 | 14 | |
| α-helix | 47-55 | 9 | |
| α-helix | 62-86 | 25 | |
| α-helix | 93-105 | 13 | |
| α-helix | 123-125 | 3 | |
| α-helix | 128-129 | 2 | |
| α-helix | 130-134 | 5 | |
| α-helix | 138-140 | 3 | |
| α-helix | 142-156 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 254-257 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin beta-4B chain | B | protein | 445 | Bos taurus | Q3MHM5 (AlphaFold model) |
| Stabilizer of axonemal microtubules 1 | D | protein | 477 | Bos taurus | A0A3S5ZPV0 (AlphaFold model) |
| Sperm acrosome associated 9 | C | protein | 224 | Bos taurus | A0A3Q1MYU9 (AlphaFold model) |
| Tubulin alpha-3 chain | A | protein | 450 | Bos taurus | Q32KN8 (AlphaFold model) |
>8OU0_1 Tubulin beta-4B chain (chains B) MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGKYV PRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS EYQQYQDATAEEEGEFEEEAEEEVA
>8OU0_2 Stabilizer of axonemal microtubules 1 (chains D) MAPTKGKCVCELCSCGRHHCPHLPTKIYDKTEKPCLLSEYTENYPVYHSYLPRESFKPKM DYQRACTPMEGLTTSRRDFGPHKVLPVKIHQPNPFVPSEENMDLQTTYKQDYNPYPLCRV DPFKPRDSKYPCGDKMESLPTYKADYLPWNQPRRELLRPPHHYRPASTKFDSRTTQQDDY SMKGLVNTRSCKPPAVPKLCNVPLEDLTNYKMSYVAHPLEKRFVHESEKFRPCEIPFESL TTHKESYRGLMGEPAKSLKPPARPYGLDTPFSNTTEFRDKYQAWPTPQVFSKPPSMYVPP EEKMDLLTTVQTHYTYPKGAPAESCRPALSVKKGGRFEGSTTTKEDYKQWASTRTEPAKP IPQLNLPTEPLDCLTTARAHYVPHLPMMTKSCKPVWSGPQGNIPVEGQTTYTISFTPKEM SRCLASYPEPPGYIFEEIDALGHRIYRPVSQTGSRRSSRFSVGDSENPNQQELTVSA
>8OU0_3 Sperm acrosome associated 9 (chains C) MMNEVKESLRSVEQKYKIFQQQQFTFIGALEHCRENAHDKIRPISSIGQVQSYMEHHCSN STDRRILLMFLDICSELSKLCQHFEALHAGTPVTNNLLEKCKTLVSQSNDLSSLRAKYPH DVVNHLSCDEARNHYGGVVSLIPIILDLMKEWVAHSEKLPRKALQQVSEPQAATRATAHA PQASGTQPQLRKQNCGQLIQNIPKPGGKDQGSSKPPWRPPGGKL
>8OU0_4 Tubulin alpha-3 chain (chains A) MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK HVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLD RIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTA VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN QMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKLDLMYAKRAFVHWYVGEGMEEGEFSE AREDLAALEKDYEEVGVDSVEAEAEEGEEY
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 1 |
| MG | Magnesium ion | Mg | 1 |
Structural specializations of the sperm tail. Leung, M.R., Zeng, J., Wang, X. et al. Cell (2023) 186:2880-2896.e17. DOI 10.1016/j.cell.2023.05.026 · PubMed
Other PDB entries of the same protein (UniProt Q3MHM5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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