2IE4: Protein Phosphatase 2A Core Enzyme

Structure of the Protein Phosphatase 2A Core Enzyme Bound to okadaic acid. Determined by X-ray diffraction at 2.6 Å resolution. Released 7 Nov 2006.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,972
Mol. weight: 101.93 kDa
Ligands: OKA, MN
Released: 7 Nov 2006

Explore 2IE4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2IE4 contains 74 α-helices and 17 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: 60 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	13-15	3
β-strand	17	1	1
β-strand	27	1	1
α-helix	29-32	4
α-helix	35-41	7
α-helix	44-46	3
α-helix	47-51	5
α-helix	52-56	5
α-helix	64-73	10
α-helix	78-80	3
α-helix	83-89	7
α-helix	90-97	8
α-helix	102-116	15
α-helix	121-123	3
α-helix	124-128	5
α-helix	129-136	8
α-helix	142-145	4
α-helix	147-150	4
α-helix	151-154	4
α-helix	160-174	15
α-helix	179-194	16
α-helix	198-200	3
α-helix	201-205	5
α-helix	206-213	8
α-helix	218-234	17
α-helix	237-243	7
α-helix	245-251	7
α-helix	257-265	9
α-helix	267-274	8
α-helix	276-278	3
α-helix	279-283	5
α-helix	284-290	7
α-helix	296-311	16
α-helix	318-321	4
α-helix	322-326	5
α-helix	327-333	7
α-helix	339-346	8
α-helix	349-355	7
α-helix	357-360	4
α-helix	361-365	5
α-helix	366-373	8
α-helix	378-385	8
α-helix	389-394	6
α-helix	397-412	16
α-helix	417-434	18
α-helix	436-438	3
α-helix	439-443	5
α-helix	444-449	6
α-helix	450-452	3
α-helix	456-473	18
α-helix	475-481	7
α-helix	483-487	5
α-helix	488-491	4
α-helix	495-520	26
α-helix	522-527	6
α-helix	528-530	3
α-helix	534-547	14
α-helix	548-550	3
α-helix	553-555	3
α-helix	556-560	5
α-helix	561-567	7
α-helix	573-586	14

Chain C: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
α-helix	25-41	17
β-strand	46-48	3	2
α-helix	49	1
β-strand	52-55	4	3
α-helix	62-72	11
β-strand	80-82	3	3
α-helix	93-106	14
β-strand	111-113	3	3
α-helix	123-125	3
α-helix	129-136	8
α-helix	141-149	9
β-strand	157-159	3	2
β-strand	163-165	3	2
α-helix	177-181	5
α-helix	188-190	3
α-helix	194-200	7
β-strand	202-203	2	4
β-strand	209-211	3	4
β-strand	218-220	3	4
α-helix	222-231	10
β-strand	236-239	4	2
β-strand	246-247	2	3
β-strand	248-251	4	2
β-strand	256-259	4	2
α-helix	265-267	3
β-strand	272-278	7	3
β-strand	284-289	6	3
α-helix	290-292	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform	A	protein	589	Homo sapiens	P30153 (AlphaFold model)
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform	C	protein	309	Homo sapiens	P67775 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2IE4_1 Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform (chains A)
MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIY
DEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHS
PSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPM
VRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDL
EALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRA
AASHKVKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDN
TIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVR
LAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHA
TIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNV
AKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA

Sequence of entity 2 (C), FASTA

>2IE4_2 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C)
MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHG
QFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHES
RQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHI
RALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRA
HQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHV
TRRTPDYFL

Ligands and cofactors

ID	Name	Formula	Copies
OKA	Okadaic acid	C44 H68 O13	1
MN	Manganese (II) ion	Mn	2

Primary citation

Structure of Protein Phosphatase 2A Core Enzyme Bound to Tumor-Inducing Toxins. Xing, Y., Xu, Y., Chen, Y. et al. Cell (2006) 127:341-353. DOI 10.1016/j.cell.2006.09.025 · PubMed

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
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
4I5N 2.8 Å, Structural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6…

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