2NPP: Protein Phosphatase 2A Holoenzyme

Structure of the Protein Phosphatase 2A Holoenzyme. Determined by X-ray diffraction at 3.3 Å resolution. Released 12 Dec 2006.

Method

X-ray diffraction

Resolution

3.3 Å

Organisms

Homo sapiens, Cyanobacteria

Chains

8

Atoms

20,466

Mol. weight

309.67 kDa

Ligands

MN

Released

12 Dec 2006

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

Secondary structure: helices and β-sheets

2NPP contains 196 α-helices and 32 β-strands across 6 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: 55 helices, 0 β-strands

Molecules and chains

>2NPP_1 Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform (chains A, D)
MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIY
DEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHS
PSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPM
VRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDL
EALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRA
AASHKVKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDN
TIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVR
LAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHA
TIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNV
AKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA

>2NPP_2 Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (chains B, E)
MLTCNKAGSRMVVDAANSNGPFQPVVLLHIRDVPPADQEKLFIQKLRQCCVLFDFVSDPL
SDLKWKEVKRAALSEMVEYITHNRNVITEPIYPEVVHMFAVNMFRTLPPSSNPTGAEFDP
EEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLQLLELFDSEDPRERD
FLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIYETEHHNGIAELLEILGSIINGFALPLK
EEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEKDSTLTEPVVMALLKYWPKTHSPK
EVMFLNELEEILDVIEPSEFVKIMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLIS
DNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQFKAEKLKEK
LKMKEREEAWVKIENLAKANPQVLKKRIT

>2NPP_3 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C, F)
MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHG
QFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHES
RQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHI
RALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRA
HQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHV
TRRTPDYFL

>2NPP_4 microcystin LR (chains X, Y)
ALDRXEX

Ligands and cofactors

Primary citation

Structure of the protein phosphatase 2A holoenzyme. Xu, Y., Xing, Y., Chen, Y. et al. Cell (2006) 127:1239-1251. DOI 10.1016/j.cell.2006.11.033 · PubMed

Related structures

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

• 1B3U 2.3 Å, Crystal structure of constant regulatory domain of human PP2A, PR65ALPHA
• 4I5L 2.43 Å, Structural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6…
• 8TWE 2.55 Å, Cryo-EM structure of the PP2A:B55-FAM122A complex, B55 body
• 2IE4 2.6 Å, Structure of the Protein Phosphatase 2A Core Enzyme Bound to okadaic acid
• 9C6B 2.6 Å, PP2A:B55-p107 substrate complex
• 8TWI 2.69 Å, Cryo-EM structure of the PP2A:B55-FAM122A complex, PP2Ac body
• 8U1X 2.7 Å, The structure of the PP2A-B56Delta holoenzyme mutant - E197K
• 9C7T 2.7 Å, PP2A:B55-Eya3 substrate complex
• 8TTB 2.77 Å, Cryo-EM structure of the PP2A:B55-ARPP19 complex
• 8SO0 2.8 Å, Cryo-EM structure of the PP2A:B55-FAM122A complex
• 2IE3 2.8 Å, Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor-inducing Toxins
• 3C5W 2.8 Å, Complex between PP2A-specific methylesterase PME-1 and PP2A core enzyme

Browse structure collections

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