2NYM: Protein phosphatase 2
Crystal Structure of Protein Phosphatase 2A (PP2A) with C-terminus truncated catalytic subunit. Determined by X-ray diffraction at 3.6 Å resolution. Released 12 Dec 2006.
- Method
- X-ray diffraction
- Resolution
- 3.6 Å
- Organisms
- Homo sapiens, Cyanobacteria
- Chains
- 8
- Atoms
- 20,212
- Mol. weight
- 293.25 kDa
- Ligands
- MN
- Released
- 12 Dec 2006
Explore 2NYM in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2NYM contains 197 α-helices and 34 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: 54 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-16 | 6 | |
| α-helix | 25-33 | 9 | |
| α-helix | 35-40 | 6 | |
| α-helix | 47-51 | 5 | |
| α-helix | 52-56 | 5 | |
| α-helix | 63-73 | 11 | |
| α-helix | 76-79 | 4 | |
| α-helix | 83-88 | 6 | |
| α-helix | 90-96 | 7 | |
| α-helix | 102-116 | 15 | |
| α-helix | 121-126 | 6 | |
| α-helix | 128-136 | 9 | |
| α-helix | 141-148 | 8 | |
| α-helix | 155-157 | 3 | |
| α-helix | 160-174 | 15 | |
| α-helix | 179-193 | 15 | |
| α-helix | 198-200 | 3 | |
| α-helix | 201-205 | 5 | |
| α-helix | 206-212 | 7 | |
| α-helix | 218-231 | 14 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-244 | 5 | |
| α-helix | 245-253 | 9 | |
| α-helix | 257-265 | 9 | |
| α-helix | 267-274 | 8 | |
| α-helix | 278 | 1 | |
| α-helix | 279-283 | 5 | |
| α-helix | 284-291 | 8 | |
| α-helix | 296-310 | 15 | |
| α-helix | 318-321 | 4 | |
| α-helix | 322-326 | 5 | |
| α-helix | 327-333 | 7 | |
| α-helix | 339-345 | 7 | |
| α-helix | 349-352 | 4 | |
| α-helix | 353-360 | 8 | |
| α-helix | 361-365 | 5 | |
| α-helix | 366-373 | 8 | |
| α-helix | 378-385 | 8 | |
| α-helix | 388-391 | 4 | |
| α-helix | 397-403 | 7 | |
| α-helix | 405-411 | 7 | |
| α-helix | 417-434 | 18 | |
| α-helix | 436-442 | 7 | |
| α-helix | 444-450 | 7 | |
| α-helix | 456-481 | 26 | |
| α-helix | 495-508 | 14 | |
| α-helix | 509-511 | 3 | |
| α-helix | 514-520 | 7 | |
| α-helix | 522-527 | 6 | |
| α-helix | 534-546 | 13 | |
| α-helix | 553-555 | 3 | |
| α-helix | 556-560 | 5 | |
| α-helix | 561-563 | 3 | |
| α-helix | 573-580 | 8 | |
Chain B: 26 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 39-42 | 4 | |
| α-helix | 59-70 | 12 | |
| α-helix | 84-92 | 9 | |
| α-helix | 96-100 | 5 | |
| α-helix | 110-112 | 3 | |
| α-helix | 113-115 | 3 | |
| α-helix | 117-118 | 2 | |
| α-helix | 121-135 | 15 | |
| α-helix | 151-159 | 9 | |
| α-helix | 167-180 | 14 | |
| α-helix | 187-203 | 17 | |
| α-helix | 211-222 | 12 | |
| α-helix | 233-236 | 4 | |
| α-helix | 237-241 | 5 | |
| α-helix | 242-245 | 4 | |
| α-helix | 249-252 | 4 | |
| α-helix | 254-266 | 13 | |
| α-helix | 272-282 | 11 | |
| α-helix | 288-302 | 15 | |
| α-helix | 307-325 | 19 | |
| α-helix | 330-337 | 8 | |
| α-helix | 338-341 | 4 | |
| α-helix | 343-351 | 9 | |
| α-helix | 353-364 | 12 | |
| α-helix | 376-388 | 13 | |
| α-helix | 392-411 | 20 | |
Chain C: 14 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-19 | 13 | |
| α-helix | 22-24 | 3 | |
| α-helix | 25-40 | 16 | |
| β-strand | 45-48 | 4 | 1 |
| α-helix | 49 | 1 | |
| β-strand | 52-55 | 4 | 2 |
| β-strand | 57 | 1 | 3 |
| α-helix | 62-72 | 11 | |
| β-strand | 80-83 | 4 | 2 |
| α-helix | 93-106 | 14 | |
| β-strand | 111-114 | 4 | 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 | 194-198 | 5 | |
| β-strand | 202-204 | 3 | 4 |
| β-strand | 211 | 1 | 5 |
| β-strand | 218 | 1 | 5 |
| β-strand | 219-221 | 3 | 4 |
| α-helix | 222-232 | 11 | |
| β-strand | 236-239 | 4 | 1 |
| β-strand | 246-247 | 2 | 2 |
| β-strand | 248-251 | 4 | 1 |
| β-strand | 256-259 | 4 | 1 |
| β-strand | 260 | 1 | 3 |
| α-helix | 265-268 | 4 | |
| β-strand | 272-278 | 7 | 2 |
| β-strand | 284-289 | 6 | 2 |
| α-helix | 290-293 | 4 | |
Chain D: 59 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-19 | 9 | |
| α-helix | 25-33 | 9 | |
| α-helix | 35-40 | 6 | |
| α-helix | 47-51 | 5 | |
| α-helix | 52-56 | 5 | |
| α-helix | 63-72 | 10 | |
| α-helix | 86-88 | 3 | |
| α-helix | 90-96 | 7 | |
| α-helix | 102-114 | 13 | |
| α-helix | 121-123 | 3 | |
| α-helix | 124-128 | 5 | |
| α-helix | 129-137 | 9 | |
| α-helix | 141-147 | 7 | |
| α-helix | 148-150 | 3 | |
| α-helix | 155-157 | 3 | |
| α-helix | 160-174 | 15 | |
| α-helix | 179-193 | 15 | |
| α-helix | 198-200 | 3 | |
| α-helix | 201-205 | 5 | |
| α-helix | 206-213 | 8 | |
| α-helix | 218-234 | 17 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-244 | 5 | |
| α-helix | 245-253 | 9 | |
| α-helix | 257-265 | 9 | |
| α-helix | 267-274 | 8 | |
| α-helix | 278 | 1 | |
| 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 | 327-333 | 7 | |
| α-helix | 339-346 | 8 | |
| α-helix | 349-352 | 4 | |
| α-helix | 353-360 | 8 | |
| α-helix | 361-365 | 5 | |
| α-helix | 366-373 | 8 | |
| α-helix | 378-385 | 8 | |
| α-helix | 388-391 | 4 | |
| α-helix | 397-403 | 7 | |
| α-helix | 405-411 | 7 | |
| α-helix | 417-434 | 18 | |
| α-helix | 436-442 | 7 | |
| α-helix | 444-449 | 6 | |
| α-helix | 450-452 | 3 | |
| α-helix | 456-473 | 18 | |
| α-helix | 475-481 | 7 | |
| α-helix | 495-508 | 14 | |
| α-helix | 509-511 | 3 | |
| α-helix | 514-520 | 7 | |
| 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 | 561-563 | 3 | |
| α-helix | 573-583 | 11 | |
Chain E: 29 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 39-42 | 4 | |
| α-helix | 59-70 | 12 | |
| α-helix | 84-92 | 9 | |
| α-helix | 96-100 | 5 | |
| α-helix | 110-112 | 3 | |
| α-helix | 113-115 | 3 | |
| α-helix | 117-118 | 2 | |
| α-helix | 121-135 | 15 | |
| α-helix | 142-144 | 3 | |
| α-helix | 151-159 | 9 | |
| α-helix | 167-180 | 14 | |
| α-helix | 187-199 | 13 | |
| α-helix | 200-204 | 5 | |
| α-helix | 211-222 | 12 | |
| α-helix | 231-236 | 6 | |
| α-helix | 237-241 | 5 | |
| α-helix | 242-245 | 4 | |
| α-helix | 249-252 | 4 | |
| α-helix | 254-266 | 13 | |
| α-helix | 269-271 | 3 | |
| α-helix | 272-282 | 11 | |
| α-helix | 288-302 | 15 | |
| α-helix | 307-325 | 19 | |
| α-helix | 330-337 | 8 | |
| α-helix | 338-341 | 4 | |
| α-helix | 343-351 | 9 | |
| α-helix | 353-364 | 12 | |
| α-helix | 376-388 | 13 | |
| α-helix | 392-411 | 20 | |
Chain F: 15 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-19 | 13 | |
| α-helix | 22-24 | 3 | |
| α-helix | 25-40 | 16 | |
| β-strand | 45-48 | 4 | 6 |
| α-helix | 49 | 1 | |
| β-strand | 52-55 | 4 | 7 |
| α-helix | 62-72 | 11 | |
| β-strand | 80-83 | 4 | 7 |
| α-helix | 93-105 | 13 | |
| β-strand | 111-114 | 4 | 7 |
| α-helix | 121-127 | 7 | |
| α-helix | 129-137 | 9 | |
| α-helix | 141-152 | 12 | |
| β-strand | 156-159 | 4 | 6 |
| β-strand | 163-166 | 4 | 6 |
| α-helix | 177-182 | 6 | |
| α-helix | 188-190 | 3 | |
| α-helix | 194-198 | 5 | |
| β-strand | 202-204 | 3 | 8 |
| β-strand | 211 | 1 | 9 |
| β-strand | 218 | 1 | 9 |
| β-strand | 219-221 | 3 | 8 |
| α-helix | 222-232 | 11 | |
| β-strand | 236-239 | 4 | 6 |
| β-strand | 246-247 | 2 | 7 |
| β-strand | 248-251 | 4 | 6 |
| β-strand | 256-259 | 4 | 6 |
| α-helix | 265-268 | 4 | |
| β-strand | 272-278 | 7 | 7 |
| β-strand | 284-289 | 6 | 7 |
| α-helix | 290-293 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein phosphatase 2 | A, D | protein | 582 | Homo sapiens | P30153 (AlphaFold model) |
| Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform | B, E | protein | 388 | Homo sapiens | Q13362 (AlphaFold model) |
| Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform | C, F | protein | 293 | Homo sapiens | P67775 (AlphaFold model) |
| microcystin LR | G, H | protein | 7 | Cyanobacteria | |
Sequence of entity 1 (A, D), FASTA
>2NYM_1 Protein phosphatase 2 (chains A, D)
DSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLL
ALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAH
FVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAAS
KLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPT
LRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVK
EFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNTIEHLLP
LFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYM
PLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVL
AMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKI
GPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA
Sequence of entity 2 (B, E), FASTA
>2NYM_2 Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (chains B, E)
QEKLFIQKLRQCCVLFDFVSDPLSDLKWKEVKRAALSEMVEYITHNRNVITEPIYPEVVH
MFAVNMFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKK
YIDQKFVLQLLELFDSEDPRERDFLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIYETEH
HNGIAELLEILGSIINGFALPLKEEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEK
DSTLTEPVVMALLKYWPKTHSPKEVMFLNELEEILDVIEPSEFVKIMEPLFRQLAKCVSS
PHFQVAERALYYWNNEYIMSLISDNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLF
MEMNQKLFDDCTQQFKAEKLKEKLKMKE
Sequence of entity 3 (C, F), FASTA
>2NYM_3 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C, F)
DEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQ
FHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESR
QITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIR
ALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAH
QLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPR
Sequence of entity 4 (G, H), FASTA
>2NYM_4 microcystin LR (chains G, H)
ALDRXEX
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MN | Manganese (II) ion | Mn | 4 |
Primary citation
Structure of the Protein Phosphatase 2A Holoenzyme. Xu, Y., Xing, Y., Chen, Y. et al. Cell (2006) 127:1239-1251. DOI 10.1016/j.cell.2006.11.033 · 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
- 3C5W 2.8 Å, Complex between PP2A-specific methylesterase PME-1 and PP2A core enzyme
Browse structure collections
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