8U89: PP2A-B56Delta holoenzyme mutant - E197K

The structure of the PP2A-B56Delta holoenzyme mutant - E197K. Determined by electron microscopy at 3.3 Å resolution. Released 10 Jan 2024.

Method
Electron microscopy
Resolution
3.3 Å
Organism
Homo sapiens
Chains
3
Atoms
9,928
Mol. weight
171.21 kDa
Ligands
MN
Released
10 Jan 2024

Explore 8U89 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8U89 contains 102 α-helices and 16 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: 60 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix25-339
α-helix35-417
α-helix461
α-helix47-515
α-helix52-576
α-helix63-7210
α-helix73-753
α-helix77-804
α-helix83-897
α-helix90-967
α-helix102-11817
α-helix121-1233
α-helix124-1285
α-helix129-1368
α-helix141-1488
α-helix160-17415
α-helix179-19315
α-helix198-2003
α-helix201-2055
α-helix206-2138
α-helix218-23316
α-helix237-2437
α-helix245-2528
α-helix257-2659
α-helix267-2748
α-helix276-2783
α-helix279-2835
α-helix284-2918
α-helix296-3049
α-helix306-3116
α-helix315-3173
α-helix318-3214
α-helix322-3265
α-helix327-3348
α-helix339-3468
α-helix349-3524
α-helix353-3564
α-helix358-3603
α-helix361-3655
α-helix366-3738
α-helix378-3869
α-helix388-3925
α-helix397-4037
α-helix405-4117
α-helix417-43418
α-helix436-4427
α-helix444-4496
α-helix450-4523
α-helix456-47318
α-helix475-4817
α-helix483-4875
α-helix488-4914
α-helix495-51622
α-helix517-5215
α-helix522-5287
α-helix534-54714
α-helix553-5553
α-helix556-5605
α-helix561-5677
α-helix573-58614
Chain B: 28 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix114-12310
α-helix128-1292
α-helix139-15820
α-helix168-17912
α-helix182-1865
α-helix196-1983
α-helix199-2013
α-helix207-22216
α-helix228-2314
α-helix237-2459
α-helix246-2483
α-helix252-26817
α-helix273-28614
α-helix287-2915
α-helix297-30812
α-helix317-3226
α-helix323-3275
α-helix329-3324
α-helix336-35318
α-helix355-3573
α-helix358-36710
α-helix374-38815
α-helix393-41220
α-helix416-4238
α-helix424-4274
α-helix429-4379
α-helix439-45214
α-helix460-47617
Chain C: 14 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix4-1714
α-helix22-243
α-helix25-3915
β-strand47-4821
β-strand52-5542
β-strand5713
α-helix62-7211
β-strand80-8232
α-helix93-10614
β-strand111-11332
α-helix121-1266
α-helix130-1378
α-helix141-15010
β-strand156-15941
β-strand163-16641
α-helix177-1815
α-helix188-1903
α-helix194-2007
β-strand202-20324
β-strand210-21124
β-strand218-22034
α-helix222-23211
β-strand236-23941
β-strand248-25141
β-strand256-25941
β-strand26013
α-helix265-2673
β-strand273-27862
β-strand284-28962
α-helix290-2945

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformAprotein589Homo sapiensP30153 (AlphaFold model)
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoformBprotein602Homo sapiensQ14738 (AlphaFold model)
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformCprotein309Homo sapiensP67775 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8U89_1 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (chains A)
MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIY
DEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHS
PSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPM
VRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDL
EALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRA
AASHKVKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDN
TIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVR
LAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHA
TIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNV
AKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA
Sequence of entity 2 (B), FASTA
>8U89_2 Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (chains B)
MPYKLKKEKEPPKVAKCTAKPSSSGKDGGGENTEEAQPQPQPQPQPQAQSQPPSSNKRPS
NSTPPPTQLSKIKYSGGPQIVKKERRQSSSRFNLSKNRELQKLPALKDSPTQEREELFIQ
KLRQCCVLFDFVSDPLSDLKFKEVKRAGLNEMVEYITHSRDVVTEAIYPEAVTMFSVNLF
RTLPPSSNPTGAEFDPKEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFV
LALLDLFDSEDPRERDFLKTILHRIYGKFLGLRAYIRRQINHIFYRFIYETEHHNGIAEL
LEILGSIINGFALPLKEEHKMFLIRVLLPLHKVKSLSVYHPQLAYCVVQFLEKESSLTEP
VIVGLLKFWPKTHSPKEVMFLNELEEILDVIEPSEFSKVMEPLFRQLAKCVSSPHFQVAE
RALYYWNNEYIMSLISDNAARVLPIMFPALYRNSKSHWNKTIHGLIYNALKLFMEMNQKL
FDDCTQQYKAEKQKGRFRMKEREEMWQKIEELARLNPQYPMFRAPPPLPPVYSMETETPT
AEDIQLLKRTVETEAVQMLKDIKKEKVLLRRKSELPQDVYTIKALEAHKRAEEFLTASQE
AL
Sequence of entity 3 (C), FASTA
>8U89_3 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C)
MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHG
QFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHES
RQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHI
RALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRA
HQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHV
TRRTPDYFL

Ligands and cofactors

IDNameFormulaCopies
MNManganese (II) ionMn2

Primary citation

B56 delta long-disordered arms form a dynamic PP2A regulation interface coupled with global allostery and Jordan's syndrome mutations. Wu, C.G., Balakrishnan, V.K., Merrill, R.A. et al. Proc Natl Acad Sci U S A (2024) 121:e2310727120-e2310727120. DOI 10.1073/pnas.2310727120 · PubMed

Other PDB entries of the same protein (UniProt P30153 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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