2YN0: Tau55 histidine phosphatase domain

tau55 histidine phosphatase domain. Determined by X-ray diffraction at 1.5 Å resolution. Released 3 Apr 2013.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
SACCHAROMYCES CEREVISIAE
Chains
1
Atoms
2,381
Mol. weight
31.14 kDa
Ligands
PO4
Released
3 Apr 2013

Explore 2YN0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2YN0 contains 15 α-helices and 9 β-strands across 1 chain. 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: 15 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand5-1061
β-strand1412
α-helix15-173
α-helix22-265
α-helix34-352
β-strand3612
α-helix371
α-helix38-5215
β-strand61-6331
α-helix67-8014
β-strand84-8631
α-helix88-903
α-helix91-933
α-helix108-1147
β-strand11911
α-helix123-1253
α-helix136-15722
β-strand163-16861
α-helix170-18112
β-strand204-20961
α-helix210-2112
α-helix231-2333
β-strand236-24381
α-helix257-2593

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcription factor tau 55 kda subunitAprotein271SACCHAROMYCES CEREVISIAEQ12415 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2YN0_1 TRANSCRIPTION FACTOR TAU 55 KDA SUBUNIT (chains A)
MVNTIYIARHGYRSNWLPEGPYPDPLTGIDSDVPLAEHGVQQAKELAHYLLSLDNQPEAA
FASPFYRCLETVQPIAKLLEIPVYLERGIGEWYRPDRKPVIPVPAGYEILSKFFPGVISQ
EWDSTLTPNEKGETEQEMYMRFKKFWPLFIERVEKEYPNVECILLVTHAASKIALGMSLL
GYDNPRMSLNENGDKIRSGSCSLDKYEILKKSYDTIDETDDQTSFTYIPFSDRKWVLTMN
GNTEFLSSGEEMNWNFDCVAEAGSDADIKKR

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P1

Primary citation

Structural and Functional Characterization of a Phosphatase Domain within Yeast General Transcription Factor Iiic. Taylor, N.M.I., Glatt, S., Hennrich, M.L. et al. J Biol Chem (2013) 288:15110. DOI 10.1074/JBC.M112.427856 · PubMed

Other PDB entries of the same protein (UniProt Q12415 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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