2IAE: Protein phosphatase 2A (PP2A) holoenzyme
Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme. Determined by X-ray diffraction at 3.5 Å resolution. Released 26 Dec 2006.
- Method
- X-ray diffraction
- Resolution
- 3.5 Å
- Organisms
- Mus musculus, Homo sapiens, Microcystis aeruginosa
- Chains
- 8
- Atoms
- 19,955
- Mol. weight
- 300.71 kDa
- Ligands
- MN
- Released
- 26 Dec 2006
Explore 2IAE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2IAE contains 196 α-helices and 33 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: 57 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-33 | 8 | |
| α-helix | 35-37 | 3 | |
| α-helix | 46 | 1 | |
| α-helix | 47-51 | 5 | |
| α-helix | 63-75 | 13 | |
| α-helix | 83-85 | 3 | |
| α-helix | 90-97 | 8 | |
| α-helix | 102-117 | 16 | |
| 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 | 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 | 206-213 | 8 | |
| α-helix | 218-231 | 14 | |
| α-helix | 246-253 | 8 | |
| α-helix | 257-264 | 8 | |
| α-helix | 267-274 | 8 | |
| α-helix | 276-278 | 3 | |
| α-helix | 279-283 | 5 | |
| α-helix | 284-290 | 7 | |
| α-helix | 296-303 | 8 | |
| α-helix | 306-311 | 6 | |
| α-helix | 317-321 | 5 | |
| α-helix | 322-326 | 5 | |
| α-helix | 327-333 | 7 | |
| α-helix | 342-349 | 8 | |
| α-helix | 352-356 | 5 | |
| α-helix | 359-360 | 2 | |
| α-helix | 361-365 | 5 | |
| α-helix | 366-373 | 8 | |
| α-helix | 378-385 | 8 | |
| α-helix | 389-394 | 6 | |
| α-helix | 397-411 | 15 | |
| α-helix | 417-424 | 8 | |
| α-helix | 427-430 | 4 | |
| α-helix | 439-442 | 4 | |
| α-helix | 444-448 | 5 | |
| α-helix | 449-452 | 4 | |
| α-helix | 456-469 | 14 | |
| α-helix | 478-482 | 5 | |
| α-helix | 483-488 | 6 | |
| α-helix | 489-491 | 3 | |
| α-helix | 495-505 | 11 | |
| α-helix | 513-516 | 4 | |
| α-helix | 517-521 | 5 | |
| α-helix | 522-528 | 7 | |
| α-helix | 534-546 | 13 | |
| α-helix | 554-556 | 3 | |
| α-helix | 562-566 | 5 | |
| α-helix | 575-578 | 4 | |
| α-helix | 581-585 | 5 | |
Chain B: 23 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 41-50 | 10 | |
| α-helix | 67-79 | 13 | |
| α-helix | 91-103 | 13 | |
| α-helix | 105-108 | 4 | |
| α-helix | 131-146 | 16 | |
| α-helix | 152-155 | 4 | |
| α-helix | 161-168 | 8 | |
| α-helix | 176-192 | 17 | |
| α-helix | 194-212 | 19 | |
| α-helix | 221-233 | 13 | |
| α-helix | 241-245 | 5 | |
| α-helix | 246-251 | 6 | |
| α-helix | 252-256 | 5 | |
| α-helix | 260-263 | 4 | |
| α-helix | 264-277 | 14 | |
| α-helix | 279-281 | 3 | |
| α-helix | 282-291 | 10 | |
| α-helix | 298-312 | 15 | |
| α-helix | 317-336 | 20 | |
| α-helix | 340-347 | 8 | |
| α-helix | 348-351 | 4 | |
| α-helix | 353-359 | 7 | |
| α-helix | 385-398 | 14 | |
Chain C: 13 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-17 | 11 | |
| 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 | 93-105 | 13 | |
| β-strand | 113 | 1 | 2 |
| α-helix | 121-124 | 4 | |
| α-helix | 128-137 | 10 | |
| α-helix | 142-152 | 11 | |
| β-strand | 156-159 | 4 | 1 |
| β-strand | 163-166 | 4 | 1 |
| α-helix | 178-181 | 4 | |
| α-helix | 188-190 | 3 | |
| α-helix | 194-198 | 5 | |
| β-strand | 202-203 | 2 | 4 |
| β-strand | 209-211 | 3 | 4 |
| β-strand | 218-220 | 3 | 4 |
| α-helix | 222-230 | 9 | |
| 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 | 271-272 | 2 | |
| β-strand | 273-278 | 6 | 2 |
| β-strand | 284-289 | 6 | 2 |
| α-helix | 290-293 | 4 | |
Chain D: 60 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-16 | 6 | |
| α-helix | 27-32 | 6 | |
| α-helix | 35-41 | 7 | |
| α-helix | 46 | 1 | |
| α-helix | 47-51 | 5 | |
| α-helix | 52-54 | 3 | |
| α-helix | 63-75 | 13 | |
| α-helix | 86-88 | 3 | |
| α-helix | 90-96 | 7 | |
| α-helix | 102-115 | 14 | |
| α-helix | 123 | 1 | |
| α-helix | 124-128 | 5 | |
| α-helix | 129-137 | 9 | |
| α-helix | 141-149 | 9 | |
| α-helix | 160-173 | 14 | |
| α-helix | 179-195 | 17 | |
| α-helix | 198-200 | 3 | |
| α-helix | 201-205 | 5 | |
| α-helix | 206-212 | 7 | |
| α-helix | 218-234 | 17 | |
| α-helix | 237-243 | 7 | |
| α-helix | 245-251 | 7 | |
| α-helix | 257-274 | 18 | |
| 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 | 315-317 | 3 | |
| α-helix | 319-321 | 3 | |
| α-helix | 322-326 | 5 | |
| α-helix | 327-333 | 7 | |
| α-helix | 339-348 | 10 | |
| α-helix | 349-352 | 4 | |
| α-helix | 353-360 | 8 | |
| α-helix | 361-365 | 5 | |
| α-helix | 366-373 | 8 | |
| α-helix | 378-386 | 9 | |
| α-helix | 389-394 | 6 | |
| α-helix | 397-403 | 7 | |
| α-helix | 405-411 | 7 | |
| α-helix | 417-424 | 8 | |
| α-helix | 427-433 | 7 | |
| α-helix | 439-442 | 4 | |
| α-helix | 444-450 | 7 | |
| α-helix | 456-470 | 15 | |
| α-helix | 475-481 | 7 | |
| α-helix | 483-487 | 5 | |
| α-helix | 488-490 | 3 | |
| α-helix | 495-511 | 17 | |
| α-helix | 513-516 | 4 | |
| 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 | 556-560 | 5 | |
| α-helix | 561-568 | 8 | |
| α-helix | 573-580 | 8 | |
| α-helix | 582-585 | 4 | |
Chain E: 29 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 42-50 | 9 | |
| α-helix | 67-77 | 11 | |
| α-helix | 79-82 | 4 | |
| α-helix | 89-91 | 3 | |
| α-helix | 92-103 | 12 | |
| α-helix | 106-108 | 3 | |
| α-helix | 131-145 | 15 | |
| α-helix | 152-155 | 4 | |
| α-helix | 161-168 | 8 | |
| α-helix | 169-172 | 4 | |
| α-helix | 176-192 | 17 | |
| α-helix | 194-209 | 16 | |
| α-helix | 210-214 | 5 | |
| α-helix | 221-232 | 12 | |
| α-helix | 239-240 | 2 | |
| α-helix | 241-245 | 5 | |
| α-helix | 246-251 | 6 | |
| α-helix | 252-254 | 3 | |
| α-helix | 260-274 | 15 | |
| α-helix | 279-281 | 3 | |
| α-helix | 282-291 | 10 | |
| α-helix | 298-312 | 15 | |
| α-helix | 317-322 | 6 | |
| α-helix | 327-335 | 9 | |
| α-helix | 340-347 | 8 | |
| α-helix | 353-359 | 7 | |
| α-helix | 386-389 | 4 | |
| α-helix | 390-392 | 3 | |
| α-helix | 393-398 | 6 | |
Chain F: 14 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-17 | 11 | |
| α-helix | 21-24 | 4 | |
| α-helix | 25-39 | 15 | |
| β-strand | 45-48 | 4 | 5 |
| 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 | 121-124 | 4 | |
| α-helix | 129-137 | 9 | |
| α-helix | 141-152 | 12 | |
| β-strand | 156-159 | 4 | 5 |
| β-strand | 163-165 | 3 | 5 |
| α-helix | 178-181 | 4 | |
| α-helix | 189-190 | 2 | |
| α-helix | 193-198 | 6 | |
| α-helix | 201-202 | 2 | |
| β-strand | 203 | 1 | 8 |
| β-strand | 209-211 | 3 | 8 |
| β-strand | 218-220 | 3 | 8 |
| α-helix | 222-229 | 8 | |
| β-strand | 236-239 | 4 | 5 |
| β-strand | 247 | 1 | 6 |
| β-strand | 248-249 | 2 | 5 |
| β-strand | 256-259 | 4 | 5 |
| β-strand | 260 | 1 | 7 |
| β-strand | 273-278 | 6 | 6 |
| β-strand | 284-289 | 6 | 6 |
| α-helix | 291-293 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform | A, D | protein | 589 | Mus musculus | Q76MZ3 (AlphaFold model) |
| Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform | B, E | protein | 407 | Homo sapiens | Q13362 (AlphaFold model) |
| Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform | C, F | protein | 309 | Homo sapiens | P67775 (AlphaFold model) |
| microcystin-LR | M, N | protein | 7 | Microcystis aeruginosa | |
Sequence of entity 1 (A, D), FASTA
>2IAE_1 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (chains A, D)
MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIY
DEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHS
PSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPM
VRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDL
EALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRA
AASHKVKEFCENLSADCRENVIMTQILPCIKELVSDANQHVKSALASVIMGLSPILGKDN
TIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVR
LAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHA
TIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNV
AKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA
Sequence of entity 2 (B, E), FASTA
>2IAE_2 Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (chains B, E)
IRDVPPADQEKLFIQKLRQCCVLFDFVSDPLSDLKWKEVKRAALSEMVEYITHNRNVITE
PIYPEVVHMFAVNMFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPD
FQPNIAKKYIDQKFVLQLLELFDSEDPRERDFLKTTLHRIYGKFLGLRAYIRKQINNIFY
RFIYETEHHNGIAELLEILGSIINGFALPLKEEHKIFLLKVLLPLHKVKSLSVYHPQLAY
CVVQFLEKDSTLTEPVVMALLKYWPKTHSPKEVMFLNELEEILDVIEPSEFVKIMEPLFR
QLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAAKILPIMFPSLYRNSKTHWNKTIHGL
IYNALKLFMEMNQKLFDDCTQQFKAEKLKEKLKMKEREEAWVKIENL
Sequence of entity 3 (C, F), FASTA
>2IAE_3 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C, F)
MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHG
QFHDLMELFRIGGKSPDTNYLFMGDYVNRGYYSVETVTLLVALKVRYRERITILRGNHES
RQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHI
RALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRA
HQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHV
TRRTPDYFL
Sequence of entity 4 (M, N), FASTA
>2IAE_4 microcystin-LR (chains M, N)
ALDRXEX
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MN | Manganese (II) ion | Mn | 4 |
Primary citation
Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Cho, U.S., Xu, W. Nature (2007) 445:53-57. DOI 10.1038/nature05351 · PubMed
Other PDB entries of the same protein (UniProt Q76MZ3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3FGA 2.7 Å, Structural Basis of PP2A and Sgo interaction
- 2PF4 3.1 Å, Crystal structure of the full-length simian virus 40 small t antigen complexed with the…
- 6EF4 3.4 Å, Crystal structure of mouse PP2A Aalpha P179R mutant
Browse structure collections
About this viewer
MolViewer shows 2IAE 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.