4NY3: Human PTPA

Human PTPA in complex with peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 23 Jul 2014.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
4
Atoms
5,761
Mol. weight
72.55 kDa
Released
23 Jul 2014

Explore 4NY3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4NY3 contains 47 α-helices and 14 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: 23 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand27-2821
α-helix33-353
α-helix36-405
β-strand4212
α-helix43-5816
α-helix72-9019
α-helix104-12118
α-helix126-1316
α-helix132-1409
β-strand14513
β-strand150-15123
α-helix153-16816
α-helix174-1763
α-helix177-1793
α-helix180-1856
α-helix186-19813
α-helix2011
β-strand202-20323
α-helix218-2269
α-helix235-2395
α-helix241-2477
α-helix252-26312
α-helix268-2714
α-helix273-2786
α-helix284-29512
α-helix296-3005
α-helix303-3064
β-strand310-31121
β-strand31912
α-helix320-3212
Chain B: 24 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand27-2824
α-helix33-353
α-helix36-405
β-strand4215
α-helix43-5816
α-helix72-8918
α-helix92-954
α-helix104-12017
α-helix126-1316
α-helix132-1409
β-strand14516
β-strand150-15126
α-helix153-16816
α-helix174-1763
α-helix177-1793
α-helix180-1856
α-helix186-19813
α-helix2011
β-strand202-20326
α-helix218-2269
α-helix235-2395
α-helix241-2477
α-helix252-26312
α-helix268-2714
α-helix273-2786
α-helix284-29512
α-helix296-3005
α-helix303-3064
β-strand310-31124
β-strand31915
α-helix320-3212

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein phosphatase 2A activatorA, Bprotein304Homo sapiensQ15257 (AlphaFold model)
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformC, Dprotein6Homo sapiensP67775 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4NY3_1 Serine/threonine-protein phosphatase 2A activator (chains A, B)
SRNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVSEAIEKLVA
LLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVATVVPTHLAAAVPEVAVYL
KESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAIVFKVFNRYLEVMRKLQKTY
RMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILF
ITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHP
VTSG
Sequence of entity 2 (C, D), FASTA
>4NY3_2 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C, D)
TPDYFL

Primary citation

Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A. Low, C., Quistgaard, E.M., Kovermann, M. et al. Biol Chem (2014) 395:881-889. DOI 10.1515/hsz-2014-0106 · PubMed

Other PDB entries of the same protein (UniProt Q15257 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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