5XW4: Tyrosine-protein phosphatase CDC14

Crystal structure of budding yeast Cdc14p (wild type) in the apo state. Determined by X-ray diffraction at 1.85 Å resolution. Released 9 Aug 2017.

Method
X-ray diffraction
Resolution
1.85 Å
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains
2
Atoms
6,526
Mol. weight
95.28 kDa
Released
9 Aug 2017

Explore 5XW4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5XW4 contains 40 α-helices and 28 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: 20 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand10-1451
β-strand18-2251
α-helix27-293
β-strand33-3641
α-helix56-7116
α-helix73-753
β-strand79-8461
α-helix88-10619
α-helix110-1145
α-helix115-1173
α-helix123-1264
β-strand12712
α-helix134-1352
β-strand13912
α-helix141-15313
α-helix164-1707
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-helix259-27416
β-strand278-28363
α-helix288-30215
α-helix306-31611
α-helix324-34219
β-strand343-34534
β-strand35015
α-helix351-3533
β-strand35615
β-strand359-36134
α-helix362-3676
Chain B: 20 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand10-1456
β-strand18-2256
α-helix27-293
β-strand33-3646
α-helix56-7116
α-helix73-753
β-strand79-8466
α-helix88-10518
α-helix110-1145
α-helix115-1173
α-helix123-1264
β-strand12717
α-helix134-1352
β-strand13917
α-helix141-15313
α-helix164-1707
α-helix173-1753
β-strand178-18038
β-strand185-18958
α-helix190-1912
α-helix209-22012
β-strand223-22868
α-helix237-2404
β-strand245-24848
α-helix259-27416
β-strand278-28368
α-helix288-30215
α-helix306-31611
α-helix324-34219
β-strand343-34539
α-helix351-3533
β-strand359-36139
α-helix362-3676

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tyrosine-protein phosphatase CDC14A, Bprotein415Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Q00684 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5XW4_1 Tyrosine-protein phosphatase CDC14 (chains A, B)
MGSSHHHHHHSQDPNSSSARLQVDKLDYDIPTTENLYFQGSMRRSVYLDNTIEFLRGRVY
LGAYDYTPEDTDELVFFTVEDAIFYNSFHLDFGPMNIGHLYRFAVIFHEILNDPENANKA
VVFYSSASTRQRANAACMLCCYMILVQAWTPHQVLQPLAQVDPPFMPFRDAGYSNADFEI
TIQDVVYGVWRAKEKGLIDLHSFNLESYEKYEHVEFGDFNVLTPDFIAFASPQEDHPKGY
LATKSSHLNQPFKSVLNFFANNNVQLVVRLNSHLYNKKHFEDIGIQHLDLIFEDGTCPDL
SIVKNFVGAAETIIKRGGKIAVHCKAGLGRTGCLIGAHLIYTYGFTANECIGFLRFIRPG
MVVGPQQHWLYLHQNDFREWKYTTRISLKPSEAIGGLYPLISLEEYRLQKKKLKD

Primary citation

Structure and dimerization of the catalytic domain of the protein phosphatase Cdc14p, a key regulator of mitotic exit in Saccharomyces cerevisiae. Kobayashi, J., Matsuura, Y. Protein Sci (2017) 26:2105-2112. DOI 10.1002/pro.3244 · 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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