Structural Basis of PP2A and Sgo interaction. Determined by X-ray diffraction at 2.7 Å resolution. Released 22 Sept 2009.
Explore 3FGA in 3D Show helices and sheets RCSB PDB PDBe
3FGA contains 105 α-helices and 14 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-21 | 11 | |
| α-helix | 25-33 | 9 | |
| α-helix | 35-41 | 7 | |
| α-helix | 44-46 | 3 | |
| α-helix | 47-51 | 5 | |
| α-helix | 52-56 | 5 | |
| α-helix | 63-73 | 11 | |
| α-helix | 86-89 | 4 | |
| α-helix | 90-98 | 9 | |
| α-helix | 102-116 | 15 | |
| 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 | 155-157 | 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 | 206-213 | 8 | |
| α-helix | 218-232 | 15 | |
| α-helix | 237-242 | 6 | |
| α-helix | 244-251 | 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 | 296-303 | 8 | |
| α-helix | 306-311 | 6 | |
| α-helix | 318-321 | 4 | |
| 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 | 378-385 | 8 | |
| α-helix | 389-394 | 6 | |
| α-helix | 397-403 | 7 | |
| α-helix | 405-411 | 7 | |
| α-helix | 417-424 | 8 | |
| α-helix | 427-434 | 8 | |
| α-helix | 436-442 | 7 | |
| α-helix | 444-450 | 7 | |
| 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 | 561-568 | 8 | |
| α-helix | 573-585 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-38 | 12 | |
| α-helix | 53-72 | 20 | |
| α-helix | 81-93 | 13 | |
| α-helix | 96-100 | 5 | |
| α-helix | 110-112 | 3 | |
| α-helix | 121-136 | 16 | |
| α-helix | 142-145 | 4 | |
| α-helix | 151-159 | 9 | |
| α-helix | 160-162 | 3 | |
| α-helix | 166-182 | 17 | |
| α-helix | 184-200 | 17 | |
| α-helix | 201-205 | 5 | |
| α-helix | 211-224 | 14 | |
| α-helix | 231-235 | 5 | |
| α-helix | 236-241 | 6 | |
| α-helix | 243-246 | 4 | |
| α-helix | 250-252 | 3 | |
| α-helix | 254-267 | 14 | |
| α-helix | 269-271 | 3 | |
| α-helix | 272-281 | 10 | |
| α-helix | 288-302 | 15 | |
| α-helix | 307-325 | 19 | |
| α-helix | 330-337 | 8 | |
| α-helix | 338-341 | 4 | |
| α-helix | 343-350 | 8 | |
| α-helix | 353-366 | 14 | |
| α-helix | 374-388 | 15 | |
| α-helix | 399-420 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-18 | 14 | |
| α-helix | 25-39 | 15 | |
| β-strand | 45-48 | 4 | 1 |
| β-strand | 52-55 | 4 | 2 |
| α-helix | 62-72 | 11 | |
| β-strand | 80-82 | 3 | 2 |
| α-helix | 93-106 | 14 | |
| β-strand | 111-113 | 3 | 2 |
| α-helix | 121-126 | 6 | |
| α-helix | 129-137 | 9 | |
| α-helix | 141-150 | 10 | |
| β-strand | 156-159 | 4 | 1 |
| β-strand | 163-166 | 4 | 1 |
| α-helix | 177-181 | 5 | |
| α-helix | 188-190 | 3 | |
| α-helix | 194-200 | 7 | |
| β-strand | 202-203 | 2 | 3 |
| β-strand | 210-211 | 2 | 3 |
| β-strand | 218-220 | 3 | 3 |
| α-helix | 222-232 | 11 | |
| β-strand | 236-239 | 4 | 1 |
| β-strand | 248-251 | 4 | 1 |
| β-strand | 256-259 | 4 | 1 |
| α-helix | 265-267 | 3 | |
| β-strand | 273-278 | 6 | 2 |
| β-strand | 286-289 | 4 | 2 |
| α-helix | 291-293 | 3 | |
| α-helix | 302-305 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 51-93 | 43 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform | A | protein | 588 | Mus musculus | Q76MZ3 (AlphaFold model) |
| Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform | B | protein | 403 | Homo sapiens | Q13362 (AlphaFold model) |
| Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform | C | protein | 309 | Homo sapiens | P67775 (AlphaFold model) |
| Shugoshin-like 1 | D | protein | 47 | Homo sapiens | Q5FBB7 (AlphaFold model) |
| Microcystin-lr | E | protein | 7 | Microcystis aeruginosa |
>3FGA_1 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (chains A) AAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYD EDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSP SDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMV RRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLE ALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAA ASHKVKEFCENLSADCRENVIMTQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNT IEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRL AIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHAT IIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVA KSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA
>3FGA_2 Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (chains B) PPADQEKLFIQKLRQCCVLFDFVSDPLSDLKWKEVKRAALSEMVEYITHNRNVITEPIYP EVVHMFAVNMFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPN IAKKYIDQKFVLQLLELFDSEDPRERDFLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIY ETEHHNGIAELLEILGSIINGFALPLKEEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQ FLEKDSTLTEPVVMALLKYWPKTHSPKEVMFLNELEEILDVIEPSEFVKIMEPLFRQLAK CVSSPHFQVAERALYYWNNEYIMSLISDNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNA LKLFMEMNQKLFDDCTQQFKAEKLKEKLKMKEREEAWVKIENL
>3FGA_3 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C) MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHG QFHDLMELFRIGGKSPDTNYLFMGDYVNRGYYSVETVTLLVALKVRYRERITILRGNHES RQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHI RALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRA HQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHV TRRTPDYFL
>3FGA_4 Shugoshin-like 1 (chains D) PSTLLKNYQDNNKMLVLALENEKSKVKEAQDIILQLRKECYYLTCQL
>3FGA_5 MICROCYSTIN-LR (chains E) ALDRXEX
| ID | Name | Formula | Copies |
|---|---|---|---|
| MN | Manganese (II) ion | Mn | 2 |
Structure and function of the PP2A-shugoshin interaction. Xu, Z., Cetin, B., Anger, M. et al. Mol Cell (2009) 35:426-441. DOI 10.1016/j.molcel.2009.06.031 · 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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