8U1X: PP2A-B56Delta holoenzyme mutant - E197K

The structure of the PP2A-B56Delta holoenzyme mutant - E197K. Determined by electron microscopy at 2.7 Å resolution. Released 17 Jan 2024.

Method: Electron microscopy
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 3
Atoms: 11,040
Mol. weight: 171.21 kDa
Ligands: MN
Released: 17 Jan 2024

Explore 8U1X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8U1X contains 116 α-helices and 19 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: 63 helices, 0 β-strands

Element	Residues	Length
α-helix	13-19	7
α-helix	25-33	9
α-helix	35-41	7
α-helix	46	1
α-helix	47-51	5
α-helix	52-57	6
α-helix	63-72	10
α-helix	86-89	4
α-helix	90-96	7
α-helix	102-116	15
α-helix	121-123	3
α-helix	124-128	5
α-helix	129-135	7
α-helix	141-146	6
α-helix	148-150	3
α-helix	160-174	15
α-helix	179-187	9
α-helix	189-193	5
α-helix	198-200	3
α-helix	201-205	5
α-helix	206-212	7
α-helix	218-232	15
α-helix	237-239	3
α-helix	240-243	4
α-helix	245-252	8
α-helix	257-265	9
α-helix	267-274	8
α-helix	276-278	3
α-helix	279-283	5
α-helix	284-291	8
α-helix	296-304	9
α-helix	306-311	6
α-helix	318-321	4
α-helix	322-326	5
α-helix	327-333	7
α-helix	339-346	8
α-helix	349-352	4
α-helix	353-356	4
α-helix	358-360	3
α-helix	361-365	5
α-helix	366-373	8
α-helix	378-385	8
α-helix	388-392	5
α-helix	397-403	7
α-helix	405-410	6
α-helix	411-413	3
α-helix	417-434	18
α-helix	436-442	7
α-helix	444-449	6
α-helix	456-473	18
α-helix	475-477	3
α-helix	478-482	5
α-helix	483-487	5
α-helix	488-491	4
α-helix	495-516	22
α-helix	517-521	5
α-helix	522-527	6
α-helix	528-530	3
α-helix	534-546	13
α-helix	553-555	3
α-helix	556-560	5
α-helix	561-567	7
α-helix	573-585	13

Chain B: 37 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	64-68	5
β-strand	81	1	1
α-helix	103-105	3
α-helix	115-123	9
α-helix	128-129	2
α-helix	139-158	20
α-helix	168-178	11
α-helix	183-186	4
α-helix	196-198	3
α-helix	199-201	3
α-helix	207-221	15
α-helix	228-231	4
α-helix	237-244	8
α-helix	245-248	4
α-helix	252-268	17
α-helix	270-272	3
α-helix	273-286	14
α-helix	287-291	5
α-helix	297-308	12
α-helix	317-322	6
α-helix	323-327	5
α-helix	328-332	5
α-helix	336-353	18
α-helix	355-357	3
α-helix	358-365	8
α-helix	374-389	16
α-helix	393-396	4
α-helix	400-411	12
α-helix	416-422	7
α-helix	423-427	5
α-helix	429-436	8
α-helix	439-451	13
α-helix	461-474	14
α-helix	497-504	8
α-helix	505-508	4
α-helix	575-576	2
β-strand	577	1	1
α-helix	579-587	9
α-helix	595-597	3

Chain C: 16 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	4-17	14
α-helix	22-24	3
α-helix	25-39	15
β-strand	45-48	4	2
β-strand	52-54	3	3
α-helix	62-72	11
β-strand	80-81	2	3
β-strand	82	1	4
α-helix	93-106	14
β-strand	113	1	4
α-helix	123-126	4
α-helix	130-137	8
α-helix	141-149	9
α-helix	150-152	3
β-strand	156-159	4	2
β-strand	163-166	4	2
β-strand	171	1	5
β-strand	174	1	5
α-helix	177-181	5
α-helix	188-190	3
α-helix	194-197	4
β-strand	202-203	2	6
β-strand	210-211	2	6
β-strand	218-220	3	6
α-helix	222-232	11
β-strand	236-239	4	2
β-strand	248-251	4	2
β-strand	256-259	4	2
α-helix	265-267	3
β-strand	273-278	6	3
β-strand	284-289	6	3
α-helix	290-294	5
α-helix	303-305	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform	A	protein	589	Homo sapiens	P30153 (AlphaFold model)
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform	B	protein	602	Homo sapiens	Q14738 (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

>8U1X_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

>8U1X_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

>8U1X_3 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C)
MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHG
QFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHES
RQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHI
RALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRA
HQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHV
TRRTPDYFL

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	2

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:

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
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…

Browse structure collections

About this viewer

MolViewer shows 8U1X directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.