3C5W: PP2A A subunit

Complex between PP2A-specific methylesterase PME-1 and PP2A core enzyme. Determined by X-ray diffraction at 2.8 Å resolution. Released 15 Apr 2008.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 3
Atoms: 6,503
Mol. weight: 95.68 kDa
Released: 15 Apr 2008

Explore 3C5W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3C5W contains 55 α-helices and 32 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: 24 helices, 0 β-strands

Element	Residues	Length
α-helix	12-20	9
α-helix	25-32	8
α-helix	35-42	8
α-helix	46	1
α-helix	400-404	5
α-helix	405-411	7
α-helix	417-424	8
α-helix	427-434	8
α-helix	436-438	3
α-helix	443-450	8
α-helix	456-473	18
α-helix	475-477	3
α-helix	478-482	5
α-helix	483-488	6
α-helix	489-491	3
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	561-568	8
α-helix	573-585	13

Chain C: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
α-helix	22-24	3
α-helix	25-40	16
β-strand	45-48	4	1
β-strand	52-55	4	2
β-strand	57	1	3
α-helix	62-72	11
β-strand	80-82	3	2
α-helix	93-106	14
β-strand	111-113	3	2
α-helix	121-127	7
α-helix	129-137	9
α-helix	141-150	10
β-strand	156-159	4	1
β-strand	163-166	4	1
α-helix	177-182	6
α-helix	189-190	2
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	1
β-strand	248-251	4	1
α-helix	252-254	3
β-strand	256-259	4	1
β-strand	260	1	3
α-helix	265-267	3
β-strand	273-278	6	2
β-strand	284-289	6	2
α-helix	290-292	3

Chain P: 16 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	46-48	3
β-strand	52-54	3	5
β-strand	57-59	3	6
β-strand	64-66	3	6
β-strand	69-72	4	5
β-strand	78-82	5	5
α-helix	89-92	4
α-helix	93-100	8
β-strand	103-104	2	7
β-strand	106-110	5	5
β-strand	119	1	6
α-helix	128-142	15
β-strand	150-155	6	5
α-helix	156-167	12
β-strand	174-180	7	5
α-helix	184-198	15
β-strand	204-205	2	8
α-helix	208-218	11
α-helix	224-230	7
α-helix	231-233	3
β-strand	235-237	3	8
β-strand	285-287	3	8
α-helix	291-297	7
α-helix	298-302	5
α-helix	305-311	7
β-strand	316-320	5	5
α-helix	323-325	3
α-helix	328-335	8
β-strand	340-343	4	5
α-helix	351-354	4
α-helix	356-369	14
β-strand	374-375	2	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PP2A A subunit	A	protein	232	Homo sapiens	P30153 (AlphaFold model)
PP2A C subunit	C	protein	310	Homo sapiens	P67775 (AlphaFold model)
PP2A-specific methylesterase PME-1	P	protein	310	Homo sapiens	Q9Y570 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3C5W_1 PP2A A subunit (chains A)
GSHMSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERLSQSLLPAIVELAEDAKW
RVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEW
AHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVR
FNVAKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA

Sequence of entity 2 (C), FASTA

>3C5W_2 PP2A C subunit (chains C)
GMDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVH
GQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHE
SRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDH
IRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSR
AHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPH
VTRRTPDYFL

Sequence of entity 3 (P), FASTA

>3C5W_3 PP2A-specific methylesterase PME-1 (chains P)
GSHMRDFSPVPWSQYFESMEDVEVENETGKDTFRVYKSGSEGPVLLLLHGGGHSALSWAV
FTAAIISRVQCRIVALDLRSHGETKVKNPEDLSAETMAKDVGNVVEAMYGDLPPPIMLIG
HAMGGAIAVHTASSNLVPSLLGLCMIDVVEGTAMDALNSMQNFLRGRPKTFKSLENAIEW
SVKSGQIRNLESARVSMVGQVKQCEGKPYTWRIELAKTEKYWDGWFRGLSNLFLSCPIPK
LLLLAGVDRLDKDLTIGQMQGKFQMQVLPQCGHAVHEDAPDKVAEAVATFLIRHRFAEPI
GGFQCVFPGC

Primary citation

Structural mechanism of demethylation and inactivation of protein phosphatase 2A. Xing, Y., Li, Z., Chen, Y. et al. Cell (2008) 133:154-163. DOI 10.1016/j.cell.2008.02.041 · 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
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
4I5N 2.8 Å, Structural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6…

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