6RFD: N-terminal DC repeat (NDC) of NDC-NDC chimera

Cryo-EM structure of the N-terminal DC repeat (NDC) of NDC-NDC chimera (human sequence) bound to 14-protofilament GDP-microtubule. Determined by electron microscopy at 3.9 Å resolution. Released 13 May 2020.

Method
Electron microscopy
Resolution
3.9 Å
Organisms
Bos taurus, Homo sapiens
Chains
5
Atoms
14,407
Mol. weight
206.18 kDa
Ligands
GDP, MG, GTP
Released
13 May 2020

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

Secondary structure: helices and β-sheets

6RFD contains 97 α-helices and 79 β-strands across 5 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 and A: 24 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand5-953
α-helix10-2617
α-helix49-513
β-strand53-5534
β-strand61-6334
β-strand65-6843
α-helix73-797
α-helix89-913
β-strand92-9323
α-helix103-1042
α-helix105-1095
α-helix111-12616
β-strand134-13853
α-helix1441
α-helix145-1495
α-helix150-16011
β-strand165-17283
α-helix173-1742
α-helix183-19412
β-strand200-20563
α-helix206-21510
α-helix224-23815
α-helix240-2434
β-strand24813
α-helix252-2598
β-strand268-27363
α-helix288-2969
α-helix307-3093
β-strand312-31433
β-strand317-32153
α-helix325-33713
β-strand34313
β-strand353-35643
α-helix358-3614
β-strand373-38193
α-helix385-40016
α-helix406-4094
α-helix417-43620
α-helix438-4392
Chain b: 23 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand3-9711
α-helix10-2718
β-strand30112
β-strand36112
α-helix47-493
β-strand51-54413
β-strand58-61413
β-strand63-67511
α-helix73-786
β-strand90-92311
α-helix101-1022
α-helix103-1075
α-helix108-1103
α-helix113-12614
β-strand130-136711
α-helix143-1475
α-helix148-15811
β-strand163-166411
β-strand169-170214
α-helix171-1722
α-helix181-19515
β-strand198-200311
β-strand202-203214
α-helix204-2096
α-helix210-2145
α-helix222-23615
β-strand246111
α-helix250-2567
β-strand265-271711
α-helix286-2927
α-helix296-2983
β-strand299111
α-helix305-3073
β-strand310-317811
β-strand318115
α-helix323-33614
β-strand341111
β-strand349-353511
α-helix356-3583
β-strand364115
β-strand365-371711
α-helix375-38915
α-helix396-3994
α-helix405-42622
Chain B: 23 helices, 22 β-strands
ElementResiduesLengthSheet
β-strand3-975
α-helix10-2718
β-strand3016
β-strand3616
α-helix47-493
β-strand51-5447
β-strand58-6147
β-strand63-6755
α-helix73-786
β-strand90-9235
α-helix101-1022
α-helix103-1075
α-helix108-1103
α-helix113-12614
β-strand130-13675
α-helix143-1475
α-helix148-15811
β-strand163-16645
β-strand169-17028
α-helix171-1722
α-helix181-19515
β-strand198-20035
β-strand202-20328
α-helix204-2096
α-helix210-2145
α-helix222-23615
β-strand24619
α-helix250-2567
β-strand265-26625
β-strand267-27159
α-helix286-2927
α-helix296-2983
β-strand29919
α-helix305-3073
β-strand310-31789
β-strand318110
α-helix323-33614
β-strand34119
β-strand349-35359
α-helix356-3583
β-strand364110
β-strand365-37179
α-helix375-38915
α-helix396-3994
α-helix405-42622
Chain N: 3 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand53-55316
β-strand56-59417
α-helix68-692
β-strand70-72316
α-helix81-899
β-strand103-106417
β-strand112117
α-helix116-1183
β-strand124-128517

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tubulin alpha-1B chainA, aprotein432Bos taurusP81947 (AlphaFold model)
Tubulin beta-2B chainB, bprotein429Bos taurusQ6B856 (AlphaFold model)
Neuronal migration protein doublecortinNprotein99Homo sapiensO43602 (AlphaFold model)
Sequence of entity 1 (A, a), FASTA
>6RFD_1 Tubulin alpha-1B chain (chains A, a)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSFNTFFSETGAGKHVPRAVFVD
LEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC
TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSIL
TTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN
VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRH
GKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA
KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALE
KDYEEVGVDSVE
Sequence of entity 2 (B, b), FASTA
>6RFD_2 Tubulin beta-2B chain (chains B, b)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDAT
Sequence of entity 3 (N), FASTA
>6RFD_3 Neuronal migration protein doublecortin (chains N)
QALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRY
IYTIDGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNV

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22
MGMagnesium ionMg2
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P32

Primary citation

Pseudo-repeats in doublecortin make distinct mechanistic contributions to microtubule regulation. Manka, S.W., Moores, C.A. EMBO Rep (2020) 21:e51534-e51534. DOI 10.15252/embr.202051534 · PubMed

Other PDB entries of the same protein (UniProt P81947 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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