6G85: Cdc14

Structure of Cdc14 bound to CBK1 PxL motif. Determined by X-ray diffraction at 1.53 Å resolution. Released 17 Oct 2018.

Method
X-ray diffraction
Resolution
1.53 Å
Organisms
Saccharomyces cerevisiae S288c, Saccharomyces cerevisiae
Chains
4
Atoms
7,063
Mol. weight
90.4 kDa
Ligands
ZN
Released
17 Oct 2018

Explore 6G85 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6G85 contains 43 α-helices and 26 β-strands across 3 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: 22 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix3-53
β-strand10-1451
β-strand18-2251
α-helix27-293
β-strand33-3641
α-helix56-7116
α-helix73-753
β-strand79-8461
α-helix88-10518
α-helix110-1145
α-helix115-1173
α-helix123-1264
β-strand12712
α-helix134-1352
β-strand13912
α-helix141-15313
α-helix164-1718
α-helix173-1753
β-strand178-18033
β-strand185-18953
α-helix190-1912
α-helix209-22012
β-strand223-22863
α-helix237-2404
β-strand245-24843
α-helix255-2584
α-helix259-27416
β-strand278-28363
α-helix288-30215
α-helix306-31611
α-helix324-34219
β-strand343-34534
α-helix351-3533
β-strand359-36134
α-helix362-37110
Chain B: 20 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand10-1455
β-strand18-2255
α-helix27-293
β-strand33-3645
α-helix56-7116
α-helix73-753
β-strand79-8465
α-helix88-10518
α-helix110-1145
α-helix115-1173
α-helix123-1264
β-strand12716
α-helix134-1352
β-strand13916
α-helix141-15313
α-helix164-1718
α-helix173-1753
β-strand178-18257
β-strand185-18957
α-helix190-1912
α-helix209-22012
β-strand223-22867
α-helix237-2404
β-strand245-24847
α-helix259-27315
β-strand278-28367
α-helix288-30215
α-helix306-31611
α-helix324-34219
β-strand343-34538
α-helix351-3533
β-strand359-36138
α-helix362-3687
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix89-924

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tyrosine-protein phosphatase CDC14A, Bprotein374Saccharomyces cerevisiae S288cQ00684 (AlphaFold model)
CBK1Cprotein16Saccharomyces cerevisiaeP53894 (AlphaFold model)
CBK1Dprotein17Saccharomyces cerevisiaeP53894 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6G85_1 Tyrosine-protein phosphatase CDC14 (chains A, B)
MRRSVYLDNTIEFLRGRVYLGAYDYTPEDTDELVFFTVEDAIFYNSFHLDFGPMNIGHLY
RFAVIFHEILNDPENANKAVVFYSSASTRQRANAACMLCCYMILVQAWTPHQVLQPLAQV
DPPFMPFRDAGYSNADFEITIQDVVYGVWRAKEKGLIDLHSFNLESYEKYEHVEFGDFNV
LTPDFIAFASPQEDHPKGYLATKSSHLNQPFKSVLNFFANNNVQLVVRLNSHLYNKKHFE
DIGIQHLDLIFEDGTCPDLSIVKNFVGAAETIIKRGGKIAVHCKAGLGRTGCLIGAHLIY
TYGFTANECIGFLRFIRPGMVVGPQQHWLYLHQNDFREWKYTTRISLKPSEAIGGLYPLI
SLEEYRLQKKKLKD
Sequence of entity 2 (C), FASTA
>6G85_2 CBK1 (chains C)
FTDVPALNYPATPPPH
Sequence of entity 3 (D), FASTA
>6G85_3 CBK1 (chains D)
AFTDVPALNYPATPPPH

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Water and common crystallization additives (PEG, EDO, GOL, MES) are not listed.

Primary citation

A PxL motif promotes timely cell cycle substrate dephosphorylation by the Cdc14 phosphatase. Kataria, M., Mouilleron, S., Seo, M.H. et al. Nat Struct Mol Biol (2018) 25:1093-1102. DOI 10.1038/s41594-018-0152-3 · PubMed

Other PDB entries of the same protein (UniProt Q00684 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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