8UWB: PP2A PPP2R1A-PPP2CA-PPP2R5E phosphatase
Crystal structure of PP2A PPP2R1A-PPP2CA-PPP2R5E phosphatase. Determined by X-ray diffraction at 3.15 Å resolution. Released 17 Apr 2024.
- Method
- X-ray diffraction
- Resolution
- 3.15 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 20,861
- Mol. weight
- 322.6 kDa
- Ligands
- MN
- Released
- 17 Apr 2024
Explore 8UWB in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8UWB contains 219 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: 62 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-20 | 7 | |
| α-helix | 25-33 | 9 | |
| α-helix | 37-42 | 6 | |
| α-helix | 44-46 | 3 | |
| α-helix | 47-51 | 5 | |
| α-helix | 52-57 | 6 | |
| α-helix | 63-73 | 11 | |
| α-helix | 82-84 | 3 | |
| α-helix | 86-88 | 3 | |
| α-helix | 90-97 | 8 | |
| α-helix | 102-115 | 14 | |
| α-helix | 121-123 | 3 | |
| α-helix | 124-128 | 5 | |
| α-helix | 129-135 | 7 | |
| α-helix | 141-147 | 7 | |
| α-helix | 151-154 | 4 | |
| α-helix | 162-174 | 13 | |
| α-helix | 179-193 | 15 | |
| α-helix | 198-201 | 4 | |
| α-helix | 205-213 | 9 | |
| α-helix | 218-232 | 15 | |
| α-helix | 240-243 | 4 | |
| α-helix | 245-252 | 8 | |
| α-helix | 257-265 | 9 | |
| α-helix | 267-274 | 8 | |
| α-helix | 277-278 | 2 | |
| α-helix | 279-283 | 5 | |
| α-helix | 284-291 | 8 | |
| α-helix | 296-304 | 9 | |
| α-helix | 306-310 | 5 | |
| α-helix | 318-321 | 4 | |
| α-helix | 322-326 | 5 | |
| α-helix | 327-334 | 8 | |
| α-helix | 339-349 | 11 | |
| α-helix | 350-352 | 3 | |
| α-helix | 353-356 | 4 | |
| α-helix | 358-360 | 3 | |
| α-helix | 361-365 | 5 | |
| α-helix | 366-373 | 8 | |
| α-helix | 378-386 | 9 | |
| α-helix | 388-394 | 7 | |
| α-helix | 397-403 | 7 | |
| α-helix | 405-411 | 7 | |
| 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 | 475-477 | 3 | |
| α-helix | 478-482 | 5 | |
| α-helix | 483-488 | 6 | |
| α-helix | 489-491 | 3 | |
| α-helix | 495-516 | 22 | |
| α-helix | 517-521 | 5 | |
| α-helix | 522-528 | 7 | |
| 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 | 573-585 | 13 | |
Chain B: 31 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 51-53 | 3 | |
| α-helix | 59-69 | 11 | |
| α-helix | 83-99 | 17 | |
| α-helix | 111-123 | 13 | |
| α-helix | 126-129 | 4 | |
| α-helix | 142-144 | 3 | |
| α-helix | 148-162 | 15 | |
| α-helix | 169-172 | 4 | |
| α-helix | 178-186 | 9 | |
| α-helix | 187-189 | 3 | |
| α-helix | 193-209 | 17 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-230 | 17 | |
| α-helix | 238-250 | 13 | |
| α-helix | 258-263 | 6 | |
| α-helix | 264-268 | 5 | |
| α-helix | 270-273 | 4 | |
| α-helix | 275-279 | 5 | |
| α-helix | 281-294 | 14 | |
| α-helix | 296-298 | 3 | |
| α-helix | 299-308 | 10 | |
| α-helix | 315-330 | 16 | |
| α-helix | 334-338 | 5 | |
| α-helix | 341-352 | 12 | |
| α-helix | 357-364 | 8 | |
| α-helix | 365-368 | 4 | |
| α-helix | 370-378 | 9 | |
| α-helix | 380-397 | 18 | |
| α-helix | 401-416 | 16 | |
| α-helix | 419-427 | 9 | |
| α-helix | 430-454 | 25 | |
Chain C: 16 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-17 | 16 | |
| α-helix | 22-24 | 3 | |
| α-helix | 25-39 | 15 | |
| 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 | 114-115 | 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 | 194-200 | 7 | |
| β-strand | 202-203 | 2 | 4 |
| β-strand | 210-211 | 2 | 4 |
| β-strand | 218-220 | 3 | 4 |
| α-helix | 222-232 | 11 | |
| β-strand | 236-239 | 4 | 1 |
| β-strand | 248-251 | 4 | 1 |
| 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 | |
| α-helix | 298-301 | 4 | |
| α-helix | 303-305 | 3 | |
Chain D: 64 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-33 | 9 | |
| α-helix | 37-42 | 6 | |
| α-helix | 44-46 | 3 | |
| α-helix | 47-51 | 5 | |
| α-helix | 52-58 | 7 | |
| α-helix | 63-73 | 11 | |
| α-helix | 77-80 | 4 | |
| α-helix | 86-89 | 4 | |
| α-helix | 90-97 | 8 | |
| α-helix | 102-115 | 14 | |
| α-helix | 121-123 | 3 | |
| α-helix | 124-128 | 5 | |
| α-helix | 129-135 | 7 | |
| α-helix | 141-147 | 7 | |
| α-helix | 151-154 | 4 | |
| α-helix | 162-174 | 13 | |
| 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 | 237-243 | 7 | |
| 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 | 378-386 | 9 | |
| α-helix | 388-394 | 7 | |
| α-helix | 397-403 | 7 | |
| α-helix | 405-411 | 7 | |
| 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 | 475-477 | 3 | |
| α-helix | 478-482 | 5 | |
| α-helix | 483-488 | 6 | |
| α-helix | 489-491 | 3 | |
| α-helix | 495-516 | 22 | |
| α-helix | 517-521 | 5 | |
| 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 | 573-585 | 13 | |
Chain E: 30 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 59-70 | 12 | |
| α-helix | 83-99 | 17 | |
| α-helix | 111-123 | 13 | |
| α-helix | 126-129 | 4 | |
| α-helix | 137-139 | 3 | |
| α-helix | 142-144 | 3 | |
| α-helix | 148-162 | 15 | |
| α-helix | 169-172 | 4 | |
| α-helix | 178-186 | 9 | |
| α-helix | 187-189 | 3 | |
| α-helix | 193-209 | 17 | |
| α-helix | 214-230 | 17 | |
| α-helix | 238-250 | 13 | |
| α-helix | 258-263 | 6 | |
| α-helix | 264-268 | 5 | |
| α-helix | 270-273 | 4 | |
| α-helix | 275-279 | 5 | |
| α-helix | 281-294 | 14 | |
| α-helix | 296-298 | 3 | |
| α-helix | 299-308 | 10 | |
| α-helix | 315-330 | 16 | |
| α-helix | 334-338 | 5 | |
| α-helix | 341-352 | 12 | |
| α-helix | 357-364 | 8 | |
| α-helix | 365-368 | 4 | |
| α-helix | 370-378 | 9 | |
| α-helix | 380-397 | 18 | |
| α-helix | 401-416 | 16 | |
| α-helix | 419-427 | 9 | |
| α-helix | 430-450 | 21 | |
Chain F: 16 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-17 | 16 | |
| α-helix | 22-24 | 3 | |
| α-helix | 25-39 | 15 | |
| β-strand | 45-48 | 4 | 5 |
| α-helix | 49 | 1 | |
| β-strand | 52-55 | 4 | 6 |
| β-strand | 57 | 1 | 7 |
| α-helix | 62-72 | 11 | |
| β-strand | 80-82 | 3 | 6 |
| α-helix | 93-106 | 14 | |
| β-strand | 111-113 | 3 | 6 |
| α-helix | 121-126 | 6 | |
| α-helix | 129-137 | 9 | |
| α-helix | 141-150 | 10 | |
| β-strand | 156-159 | 4 | 5 |
| β-strand | 163-166 | 4 | 5 |
| α-helix | 177-182 | 6 | |
| α-helix | 194-200 | 7 | |
| β-strand | 202-203 | 2 | 8 |
| β-strand | 210-211 | 2 | 8 |
| β-strand | 218-220 | 3 | 8 |
| α-helix | 222-232 | 11 | |
| β-strand | 236-239 | 4 | 5 |
| β-strand | 248-251 | 4 | 5 |
| β-strand | 256-259 | 4 | 5 |
| β-strand | 260 | 1 | 7 |
| α-helix | 265-267 | 3 | |
| α-helix | 271-272 | 2 | |
| β-strand | 273-278 | 6 | 6 |
| β-strand | 284-289 | 6 | 6 |
| α-helix | 290-292 | 3 | |
| α-helix | 303-305 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform | A, D | protein | 612 | Homo sapiens | P67775 (AlphaFold model) |
| Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform | B, E | protein | 467 | Homo sapiens | Q16537 (AlphaFold model) |
| Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform | C, F | protein | 333 | Homo sapiens | P30153 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>8UWB_1 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains A, D)
MDYKDDDDKSAVDENLYFQGGGRMAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLST
IALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLA
TVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPR
VSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQ
DSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPE
ITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMSQILPCIKELVSDA
NQHVKSALASVIMGLSPILGKDNTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGI
RQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYA
IREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDIT
TKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKY
FAQEALTVLSLA
Sequence of entity 2 (B, E), FASTA
>8UWB_2 Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform (chains B, E)
MSSAPTTPPSVDKVDGFSRKSVRKARQKRSQSSSQFRSQGKPIELTPLPLLKDVPSSEQP
ELFLKKLQQCCVIFDFMDTLSDLKMKEYKRSTLNELVDYITISRGCLTEQTYPEVVRMVS
CNIFRTLPPSDSNEFDPEEDEPTLEASWPHLQLVYEFFIRFLESQEFQPSIAKKYIDQKF
VLQLLELFDSEDPRERDYLKTVLHRIYGKFLGLRAFIRKQINNIFLRFVYETEHFNGVAE
LLEILGSIINGFALPLKAEHKQFLVKVLIPLHTVRSLSLFHAQLAYCIVQFLEKDPSLTE
PVIRGLMKFWPKTCSQKEVMFLGELEEILDVIEPSQFVKIQEPLFKQIAKCVSSPHFQVA
ERALYYWNNEYIMSLIEENSNVILPIMFSSLYRISKEHWNPAIVALVYNVLKAFMEMNST
MFDELTATYKSDRQREKKKEKEREELWKKLEDLELKRGLRRDGIIPT
Sequence of entity 3 (C, F), FASTA
>8UWB_3 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (chains C, F)
MDWSHPQFEKSAVDENLYFQGGGRMDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAK
EILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVET
VTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLT
ALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGA
GYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIM
ELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MN | Manganese (II) ion | Mn | 4 |
Primary citation
Structural characterization of methylation-independent PP2A assembly guides alphafold2Multimer prediction of family-wide PP2A complexes. Wachter, F., Nowak, R.P., Ficarro, S. et al. J Biol Chem (2024) 300:107268-107268. DOI 10.1016/j.jbc.2024.107268 · PubMed
Other PDB entries of the same protein (UniProt P67775 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4NY3 1.8 Å, Human PTPA in complex with peptide
- 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
- 3FGA 2.7 Å, Structural Basis of PP2A and Sgo interaction
- 3P71 2.7 Å, Crystal structure of the complex of LCMT-1 and PP2A
- 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
- 4IYP 2.8 Å, structure of the nPP2Ac-alpha4 complex
Browse structure collections
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