6DPU: Undecorated GMPCPP microtubule

Undecorated GMPCPP microtubule. Determined by electron microscopy at 3.1 Å resolution. Released 4 Jul 2018.

Method
Electron microscopy
Resolution
3.1 Å
Organism
Sus scrofa
Chains
12
Atoms
40,650
Mol. weight
607.23 kDa
Ligands
G2P, MG, GTP
Released
4 Jul 2018

Explore 6DPU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6DPU contains 319 α-helices and 204 β-strands across 12 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.

Chains A, C, E, J, K and L: 27 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand4-961
α-helix10-2819
α-helix48-514
β-strand53-5532
β-strand61-6332
β-strand65-6951
α-helix73-808
α-helix89-913
β-strand92-9431
α-helix103-1075
α-helix111-1133
α-helix115-12713
β-strand134-14071
α-helix1441
α-helix145-1495
α-helix150-16112
β-strand165-17281
α-helix173-1742
α-helix183-19715
β-strand200-20561
α-helix206-21712
α-helix224-24320
β-strand24813
α-helix252-2598
α-helix2681
β-strand269-27353
α-helix278-2836
α-helix288-2958
α-helix298-3003
β-strand30113
α-helix307-3093
β-strand312-321103
α-helix325-33713
β-strand34313
β-strand351-35663
α-helix359-3613
α-helix369-3702
β-strand373-38193
α-helix382-3843
α-helix385-40016
α-helix405-4106
α-helix415-43622
Chain B: 27 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-974
α-helix10-2718
β-strand3015
β-strand3516
β-strand3615
α-helix42-474
α-helix49-513
β-strand53-5646
β-strand60-6346
β-strand65-6954
α-helix72-809
α-helix84-863
α-helix89-913
β-strand92-9434
α-helix103-1075
α-helix110-12819
β-strand132-14094
α-helix145-1495
α-helix150-16011
β-strand165-17284
α-helix1731
α-helix183-19715
β-strand200-20564
α-helix206-2116
α-helix212-2165
α-helix224-24320
β-strand246-24837
α-helix252-2598
β-strand267-26824
β-strand269-27357
α-helix279-2813
α-helix288-2969
α-helix298-3003
β-strand30117
α-helix307-3093
β-strand312-321107
α-helix325-33814
α-helix340-3423
β-strand34317
β-strand351-35667
α-helix359-3602
β-strand373-38197
α-helix382-3843
α-helix385-39915
α-helix405-4106
α-helix415-43622
Chains D, F, G, H and I: 26 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-9711
α-helix10-2718
β-strand30112
β-strand35113
β-strand36112
α-helix42-474
α-helix49-513
β-strand53-56413
β-strand60-63413
β-strand65-69511
α-helix72-809
α-helix84-863
α-helix89-913
β-strand92-94311
α-helix103-1075
α-helix110-12819
β-strand132-140911
α-helix145-1495
α-helix150-16011
β-strand165-172811
α-helix183-19715
β-strand200-205611
α-helix206-2116
α-helix212-2165
α-helix224-24320
β-strand246-248314
α-helix252-2598
β-strand267-268211
β-strand269-273514
α-helix279-2813
α-helix288-2969
α-helix298-3003
β-strand301114
α-helix307-3093
β-strand312-3211014
α-helix325-33814
α-helix340-3423
β-strand343114
β-strand351-356614
α-helix359-3602
β-strand373-381914
α-helix382-3843
α-helix385-39915
α-helix405-4106
α-helix415-43622

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tubulin alpha-1B chainA, C, E, J, K, Lprotein451Sus scrofaQ2XVP4 (AlphaFold model)
Tubulin beta chainB, D, F, G, H, Iprotein445Sus scrofaP02554 (AlphaFold model)
Sequence of entity 1 (A, C, E, J, K, L), FASTA
>6DPU_1 Tubulin alpha-1B chain (chains A, C, E, J, K, L)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Sequence of entity 2 (B, D, F, G, H, I), FASTA
>6DPU_2 Tubulin beta chain (chains B, D, F, G, H, I)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEGEEDEA

Ligands and cofactors

IDNameFormulaCopies
G2PPhosphomethylphosphonic acid guanylate esterC11 H18 N5 O13 P36
MGMagnesium ionMg12
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P36

Primary citation

Separating the effects of nucleotide and EB binding on microtubule structure. Zhang, R., LaFrance, B., Nogales, E. Proc Natl Acad Sci U S A (2018) 115:E6191-E6200. DOI 10.1073/pnas.1802637115 · PubMed

Other PDB entries of the same protein (UniProt Q2XVP4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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6DPU is part of these collections:

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