Crystal structure of mouse PP2A Aalpha P179R mutant. Determined by X-ray diffraction at 3.4 Å resolution. Released 26 Jun 2019.
Explore 6EF4 in 3D Show helices and sheets RCSB PDB PDBe
6EF4 contains 62 α-helices and 0 β-strands across 1 chain. 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-19 | 3 | |
| α-helix | 25-32 | 8 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-41 | 4 | |
| α-helix | 47-51 | 5 | |
| α-helix | 52-54 | 3 | |
| α-helix | 66-72 | 7 | |
| α-helix | 86-88 | 3 | |
| α-helix | 90-96 | 7 | |
| α-helix | 105-116 | 12 | |
| α-helix | 121-123 | 3 | |
| α-helix | 124-128 | 5 | |
| α-helix | 129-136 | 8 | |
| 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 | 218-221 | 4 | |
| α-helix | 222-224 | 3 | |
| α-helix | 226-234 | 9 | |
| α-helix | 237-243 | 7 | |
| α-helix | 245-252 | 8 | |
| α-helix | 257-265 | 9 | |
| α-helix | 267-278 | 12 | |
| α-helix | 279-283 | 5 | |
| α-helix | 284-290 | 7 | |
| α-helix | 296-303 | 8 | |
| α-helix | 306-311 | 6 | |
| α-helix | 319-321 | 3 | |
| α-helix | 322-326 | 5 | |
| α-helix | 327-334 | 8 | |
| 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 | 378-386 | 9 | |
| α-helix | 389-392 | 4 | |
| α-helix | 401-403 | 3 | |
| α-helix | 405-412 | 8 | |
| α-helix | 417-425 | 9 | |
| α-helix | 427-433 | 7 | |
| α-helix | 438-442 | 5 | |
| α-helix | 444-448 | 5 | |
| α-helix | 456-471 | 16 | |
| α-helix | 475-481 | 7 | |
| α-helix | 483-487 | 5 | |
| α-helix | 488-491 | 4 | |
| α-helix | 495-509 | 15 | |
| α-helix | 515-516 | 2 | |
| α-helix | 517-521 | 5 | |
| α-helix | 522-527 | 6 | |
| α-helix | 528-530 | 3 | |
| α-helix | 534-547 | 14 | |
| α-helix | 555 | 1 | |
| α-helix | 556-560 | 5 | |
| α-helix | 561-567 | 7 | |
| α-helix | 573-580 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform | A | protein | 590 | Mus musculus | Q76MZ3 (AlphaFold model) |
>6EF4_1 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (chains A) GMAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTI YDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEH SPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTR MVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQED LEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVR AAASHKVKEFCENLSADCRENVIMTQILPCIKELVSDANQHVKSALASVIMGLSPILGKD NTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRV RLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAH ATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFN VAKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA
The Highly Recurrent PP2A A alpha-Subunit Mutation P179R Alters Protein Structure and Impairs PP2A Enzyme Function to Promote Endometrial Tumorigenesis. Taylor, S.E., O'Connor, C.M., Wang, Z. et al. Cancer Res (2019) 79:4242-4257. DOI 10.1158/0008-5472.CAN-19-0218 · PubMed
Other PDB entries of the same protein (UniProt Q76MZ3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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