9MF5: PDB entry 9MF5

CryoEM structure of the Protein Phosphatase 2A (Abeta-B56gamma-Calpha) holoenzyme complex. Determined by electron microscopy at 3.2 Å resolution. Released 9 Jul 2025.

Method
Electron microscopy
Resolution
3.2 Å
Organism
Homo sapiens
Chains
3
Atoms
9,993
Mol. weight
163.17 kDa
Ligands
MN
Released
9 Jul 2025

Explore 9MF5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9MF5 contains 95 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: 56 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix28-314
α-helix37-459
α-helix47-548
α-helix56-583
α-helix59-635
α-helix64-696
α-helix75-8410
α-helix85-873
α-helix88-914
α-helix95-1017
α-helix102-1109
α-helix114-13017
α-helix133-1353
α-helix136-1405
α-helix141-1488
α-helix153-1597
α-helix163-1664
α-helix172-18615
α-helix191-20717
α-helix210-2123
α-helix213-2175
α-helix218-2258
α-helix230-24617
α-helix249-2513
α-helix252-2565
α-helix257-2648
α-helix269-2779
α-helix279-29416
α-helix296-3038
α-helix308-32316
α-helix327-3337
α-helix334-3385
α-helix339-3468
α-helix351-36010
α-helix363-3686
α-helix370-3723
α-helix373-3775
α-helix378-3858
α-helix390-3989
α-helix400-42324
α-helix429-44618
α-helix448-4503
α-helix451-4555
α-helix456-4616
α-helix462-4643
α-helix468-48922
α-helix490-4945
α-helix495-5017
α-helix507-52822
α-helix529-5335
α-helix534-5418
α-helix546-55813
α-helix565-5673
α-helix568-5725
α-helix573-5808
α-helix585-59713
Chain B: 25 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix39-4911
α-helix63-8220
α-helix91-10313
α-helix106-1094
α-helix120-1223
α-helix131-14616
α-helix152-1587
α-helix161-1699
α-helix170-1723
α-helix176-19217
α-helix197-21014
α-helix211-2155
α-helix221-23313
α-helix241-2466
α-helix247-2515
α-helix252-2543
α-helix260-27718
α-helix282-29110
α-helix298-31215
α-helix317-33519
α-helix340-3478
α-helix348-3514
α-helix353-3608
α-helix363-37715
α-helix384-40017
Chain C: 14 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix4-1714
α-helix25-3915
β-strand45-4841
β-strand52-5542
β-strand5713
α-helix62-7211
β-strand80-8232
α-helix93-10614
β-strand111-11332
α-helix121-1266
α-helix128-13710
α-helix141-15010
β-strand156-15941
β-strand163-16641
α-helix177-1826
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
α-helix271-2722
β-strand273-27862
β-strand284-28962
α-helix291-2933
α-helix303-3053

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoformAprotein601Homo sapiensP30154 (AlphaFold model)
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoformBprotein524Homo sapiensQ13362 (AlphaFold model)
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformCprotein309Homo sapiensP67775 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9MF5_1 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (chains A)
MAGASELGTGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTR
SELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLENLATVEETVVRDKA
VESLRQISQEHTPVALEAYFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQ
QFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTSLASDEQDSVRLLAVEAC
VSIAQLLSQDDLETLVMPTLRQAAEDKSWRVRYMVADRFSELQKAMGPKITLNDLIPAFQ
NLLKDCEAEVRAAAAHKVKELGENLPIEDRETIIMNQILPYIKELVSDTNQHVKSALASV
IMGLSTILGKENTIEHLLPLFLAQLKDECPDVRLNIISNLDCVNEVIGIRQLSQSLLPAI
VELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMK
LVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGQEITTKQMLPIVLKM
AGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLAL
A
Sequence of entity 2 (B), FASTA
>9MF5_2 Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (chains B)
MLTCNKAGSRMVVDAANSNGPFQPVVLLHIRDVPPADQEKLFIQKLRQCCVLFDFVSDPL
SDLKWKEVKRAALSEMVEYITHNRNVITEPIYPEVVHMFAVNMFRTLPPSSNPTGAEFDP
EEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLQLLELFDSEDPRERD
FLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIYETEHHNGIAELLEILGSIINGFALPLK
EEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEKDSTLTEPVVMALLKYWPKTHSPK
EVMFLNELEEILDVIEPSEFVKIMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLIS
DNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQFKAEKLKEK
LKMKEREEAWVKIENLAKANPQYTVYSQASTMSIPVAMETDGPLFEDVQMLRKTVKDEAH
QAQKDPKKDRPLARRKSELPQDPHTKKALEAHCRADELASQDGR
Sequence of entity 3 (C), FASTA
>9MF5_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

Regulatory mechanisms of PP2A complex assembly driven by physicochemical differences in A-subunit isoforms. Day, A., Huang, W., Leonard, D. et al. Structure (2025) 33:1688-1699.e5. DOI 10.1016/j.str.2025.06.013 · PubMed

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