4LAC: PDB entry 4LAC

Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A phosphatase activator (PTPA) complex with ATPgammaS. Determined by X-ray diffraction at 2.82 Å resolution. Released 9 Oct 2013.

Method
X-ray diffraction
Resolution
2.82 Å
Organism
Homo sapiens
Chains
3
Atoms
6,813
Mol. weight
100.4 kDa
Ligands
AGS, MN
Released
9 Oct 2013

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

Secondary structure: helices and β-sheets

4LAC contains 61 α-helices and 23 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: 21 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix366-3738
α-helix378-40326
α-helix405-4128
α-helix417-43418
α-helix436-4427
α-helix444-4496
α-helix450-4523
α-helix456-47318
α-helix475-4817
α-helix483-4886
α-helix489-4913
α-helix495-51622
α-helix517-5215
α-helix522-5276
α-helix528-5303
α-helix534-54714
α-helix548-5503
α-helix553-5553
α-helix556-5605
α-helix561-5677
α-helix573-58513
Chain B: 23 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand2711
α-helix33-353
α-helix36-405
β-strand4212
α-helix43-5816
α-helix72-8918
α-helix92-943
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-helix208-2103
α-helix218-2269
α-helix235-2395
α-helix241-2455
α-helix252-26312
α-helix268-2714
α-helix273-2786
α-helix284-29815
α-helix303-3064
β-strand31111
β-strand31912
Chain C: 17 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix5-1814
α-helix22-243
α-helix25-4016
β-strand45-4844
α-helix491
β-strand52-5545
β-strand5716
α-helix62-7211
β-strand80-8235
α-helix93-10614
β-strand111-11335
α-helix114-1163
α-helix121-1244
α-helix129-1379
α-helix141-15010
β-strand156-15944
β-strand163-16644
α-helix177-1826
α-helix189-1902
α-helix194-2007
β-strand202-20327
β-strand209-21137
β-strand218-22037
α-helix222-23211
β-strand236-23944
β-strand248-25144
β-strand256-25944
β-strand26016
α-helix265-2673
β-strand273-27865
α-helix2791
β-strand284-28965
α-helix290-2923

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein phosphatase 2A activatorBprotein308Homo sapiensQ15257 (AlphaFold model)
PP2A Scaffold Subunit A, Truncated, an internal deletion of PP2A AAprotein258Homo sapiensP30153 (AlphaFold model)
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformCprotein311Homo sapiensP67775 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>4LAC_1 Serine/threonine-protein phosphatase 2A activator (chains B)
GSMATQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVSEAIE
KLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVATVVPTHLAAAVPEV
AVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAIVFKVFNRYLEVMRKL
QKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLE
CILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLL
PIHPVTSG
Sequence of entity 2 (A), FASTA
>4LAC_2 PP2A Scaffold Subunit A, Truncated, an internal deletion of PP2A A (chains A)
STGIASDSSSDSSSSSSSSSSDSDSECESMSLYPIAVLIDELRNEDVQLRLNSIKKLSTI
ALALGVERTRSELLPFIVELAEDAKWRVRLAIIEYMPLLAGQLGVEYFDEKLNSLCMAWL
VDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEV
CGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPILEKLTQDQ
DVDVKYFAQEALTVLSLA
Sequence of entity 3 (C), FASTA
>4LAC_3 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C)
GSMDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDV
HGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNH
ESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLD
HIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVS
RAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEP
HVTRRTPDYFL

Ligands and cofactors

IDNameFormulaCopies
AGSPhosphothiophosphoric acid-adenylate esterC10 H16 N5 O12 P3 S1
MNManganese (II) ionMn2

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

Primary citation

Structural basis of PP2A activation by PTPA, an ATP-dependent activation chaperone. Guo, F., Stanevich, V., Wlodarchak, N. et al. Cell Res (2014) 24:190-203. DOI 10.1038/cr.2013.138 · PubMed

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

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