5W3D: Kinesin-14 wild-type Ncd-ADP dimer

The structure of kinesin-14 wild-type Ncd-ADP dimer. Determined by X-ray diffraction at 2.79 Å resolution. Released 20 Dec 2017.

Method
X-ray diffraction
Resolution
2.79 Å
Organism
Drosophila melanogaster
Chains
2
Atoms
5,346
Mol. weight
94.42 kDa
Ligands
ADP, MG
Released
20 Dec 2017

Explore 5W3D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5W3D contains 31 α-helices and 37 β-strands across 2 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.

Chain A: 17 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix293-34654
β-strand349-35571
α-helix356-3594
α-helix3661
β-strand36712
β-strand369-37133
β-strand377-38153
β-strand394-39743
β-strand400-40231
α-helix408-4136
α-helix416-4238
β-strand428-43361
α-helix440-4445
β-strand446-44724
β-strand450-45124
α-helix453-46816
α-helix469-4713
β-strand473-485131
β-strand488-49141
β-strand502-50435
β-strand512-51435
β-strand520-52121
α-helix525-53814
α-helix550-5523
β-strand554-565121
β-strand570-580111
α-helix581-5833
α-helix602-61413
α-helix622-6243
α-helix626-6305
α-helix632-6343
β-strand640-64781
β-strand65012
α-helix651-6533
α-helix654-66916
Chain B: 14 helices, 19 β-strands
ElementResiduesLengthSheet
α-helix295-34551
β-strand349-35576
α-helix356-3594
α-helix3661
β-strand36717
α-helix3681
β-strand369-37248
β-strand377-38158
β-strand395-39738
β-strand400-40236
α-helix408-4136
α-helix416-4249
β-strand427-43486
α-helix440-4445
β-strand446-44729
β-strand450-45129
α-helix453-46816
β-strand474-479610
β-strand482-48436
β-strand489-49136
β-strand520-522310
α-helix525-53814
β-strand554-55636
β-strand55816
β-strand561-564410
β-strand575-58066
α-helix581-5833
α-helix601-61414
α-helix627-6304
β-strand641-64776
β-strand65017
α-helix651-6533
α-helix654-66714

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein claret segregationalA, Bprotein412Drosophila melanogasterP20480 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5W3D_1 Protein claret segregational (chains A, B)
MGSMHAALSTEVVHLRQRTEELLRCNEQQAAELETCKEQLFQSNMERKELHNTVMDLRGN
IRVFCRIRPPLESEENRMCCTWTYHDESTVELQSIDAQAKSKMGQQIFSFDQVFHPLSSQ
SDIFEMVSPLIQSALDGYNICIFAYGQTGSGKTYTMDGVPESVGVIPRTVDLLFDSIRGY
RNLGWEYEIKATFLEIYNEVLYDLLSNEQKDMEIRMAKNNKNDIYVSNITEETVLDPNHL
RHLMHTAKMNRATASTAGNERSSRSHAVTKLELIGRHAEKQEISVGSINLVDLAGSESPK
TSTRMTETKNINRSLSELTNVILALLQKQDHIPYRNSKLTHLLMPSLGGNSKTLMFINVS
PFQDCFQESVKSLRFAASVNSCKMTKAKRNRYLNNSVANSSTQSNNSGNFDK

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P22
MGMagnesium ionMg2

Primary citation

Structural basis of small molecule ATPase inhibition of a human mitotic kinesin motor protein. Park, H.W., Ma, Z., Zhu, H. et al. Sci Rep (2017) 7:15121-15121. DOI 10.1038/s41598-017-14754-6 · PubMed

Other PDB entries of the same protein (UniProt P20480 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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