7K36: STRIPAK complex
Cryo-EM structure of STRIPAK complex. Determined by electron microscopy at 3.3 Å resolution. Released 10 Mar 2021.
- Method
- Electron microscopy
- Resolution
- 3.3 Å
- Organism
- Homo sapiens
- Chains
- 9
- Atoms
- 16,613
- Mol. weight
- 612.84 kDa
- Ligands
- MN, ZN, IHP
- Released
- 10 Mar 2021
Explore 7K36 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7K36 contains 102 α-helices and 47 β-strands across 9 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: 40 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-20 | 9 | |
| α-helix | 25-33 | 9 | |
| α-helix | 35-41 | 7 | |
| α-helix | 44-46 | 3 | |
| α-helix | 47-51 | 5 | |
| α-helix | 52-57 | 6 | |
| α-helix | 63-73 | 11 | |
| α-helix | 83-85 | 3 | |
| α-helix | 86-97 | 12 | |
| α-helix | 102-115 | 14 | |
| α-helix | 123-138 | 16 | |
| α-helix | 142-154 | 13 | |
| α-helix | 156-158 | 3 | |
| α-helix | 163-174 | 12 | |
| α-helix | 179-192 | 14 | |
| α-helix | 198-213 | 16 | |
| α-helix | 218-233 | 16 | |
| α-helix | 240-252 | 13 | |
| α-helix | 258-271 | 14 | |
| α-helix | 283-290 | 8 | |
| α-helix | 298-316 | 19 | |
| α-helix | 319-334 | 16 | |
| α-helix | 342-352 | 11 | |
| α-helix | 353-355 | 3 | |
| α-helix | 360-374 | 15 | |
| α-helix | 378-394 | 17 | |
| α-helix | 401-411 | 11 | |
| α-helix | 417-433 | 17 | |
| α-helix | 436-440 | 5 | |
| α-helix | 443-451 | 9 | |
| α-helix | 456-489 | 34 | |
| α-helix | 496-512 | 17 | |
| α-helix | 514-516 | 3 | |
| α-helix | 517-521 | 5 | |
| α-helix | 522-528 | 7 | |
| α-helix | 534-547 | 14 | |
| α-helix | 553-555 | 3 | |
| α-helix | 556-560 | 5 | |
| α-helix | 561-568 | 8 | |
| α-helix | 573-586 | 14 | |
Chain B: 2 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 388-392 | 5 | 1 |
| β-strand | 401-404 | 4 | 2 |
| β-strand | 410-414 | 5 | 2 |
| β-strand | 420-424 | 5 | 2 |
| β-strand | 441-444 | 4 | 2 |
| β-strand | 454-457 | 4 | 3 |
| β-strand | 463-467 | 5 | 3 |
| β-strand | 472-477 | 6 | 3 |
| α-helix | 478-480 | 3 | |
| α-helix | 491-493 | 3 | |
| β-strand | 494-499 | 6 | 3 |
| β-strand | 505-510 | 6 | 4 |
| β-strand | 517-521 | 5 | 4 |
| β-strand | 526-529 | 4 | 4 |
| β-strand | 539-541 | 3 | 4 |
| β-strand | 553-555 | 3 | 5 |
| β-strand | 563-566 | 4 | 5 |
| β-strand | 572-575 | 4 | 5 |
| β-strand | 584-586 | 3 | 5 |
| β-strand | 600-605 | 6 | 6 |
| β-strand | 611-616 | 6 | 6 |
| β-strand | 620-625 | 6 | 6 |
| β-strand | 633-636 | 4 | 6 |
| β-strand | 642-647 | 6 | 7 |
| β-strand | 653-658 | 6 | 7 |
| β-strand | 663-667 | 5 | 7 |
| β-strand | 675-677 | 3 | 7 |
| β-strand | 690-693 | 4 | 1 |
| β-strand | 700-703 | 4 | 1 |
| β-strand | 709-712 | 4 | 1 |
Chain C: 12 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-17 | 14 | |
| α-helix | 25-39 | 15 | |
| β-strand | 45-48 | 4 | 8 |
| β-strand | 52-55 | 4 | 9 |
| α-helix | 62-72 | 11 | |
| β-strand | 80-83 | 4 | 9 |
| α-helix | 93-106 | 14 | |
| β-strand | 111-114 | 4 | 9 |
| α-helix | 117-119 | 3 | |
| α-helix | 121-127 | 7 | |
| α-helix | 129-137 | 9 | |
| α-helix | 141-150 | 10 | |
| β-strand | 156-159 | 4 | 8 |
| β-strand | 163-165 | 3 | 8 |
| α-helix | 177-181 | 5 | |
| α-helix | 195-198 | 4 | |
| β-strand | 211 | 1 | 10 |
| β-strand | 218 | 1 | 10 |
| α-helix | 222-232 | 11 | |
| β-strand | 236-239 | 4 | 8 |
| β-strand | 248-251 | 4 | 8 |
| β-strand | 256-259 | 4 | 8 |
| β-strand | 273-278 | 6 | 9 |
| β-strand | 284-289 | 6 | 9 |
| α-helix | 291-293 | 3 | |
Chain D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-134 | 70 | |
Chain E: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-126 | 62 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-122 | 58 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-120 | 56 | |
Chain H: 8 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-24 | 4 | |
| α-helix | 38-49 | 12 | |
| α-helix | 54-58 | 5 | |
| α-helix | 67-91 | 25 | |
| α-helix | 121-136 | 16 | |
| α-helix | 153-173 | 21 | |
| α-helix | 175-184 | 10 | |
| α-helix | 187-198 | 12 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform | A | protein | 589 | Homo sapiens | P30153 (AlphaFold model) |
| Striatin-3 | B, D, E, F, G | protein | 713 | Homo sapiens | Q13033 (AlphaFold model) |
| Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform | C | protein | 309 | Homo sapiens | P67775 (AlphaFold model) |
| MOB-like protein phocein | H | protein | 225 | Homo sapiens | Q9Y3A3 (AlphaFold model) |
| Striatin-interacting protein 1 | I | protein | 837 | Homo sapiens | Q5VSL9 |
Sequence of entity 1 (A), FASTA
>7K36_1 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (chains A)
MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIY
DEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHS
PSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPM
VRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDL
EALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRA
AASHKVKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDN
TIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVR
LAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHA
TIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNV
AKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA
Sequence of entity 2 (B, D, E, F, G), FASTA
>7K36_2 Striatin-3 (chains B, D, E, F, G)
MDELAGGGGGGPGMAAPPRQQQGPGGNLGLSPGGNGAAGGGGPPASEGAGPAAGPELSRP
QQYTIPGILHYIQHEWARFEMERAHWEVERAELQARIAFLQGERKGQENLKKDLVRRIKM
LEYALKQERAKYHKLKYGTELNQGDLKMPTFESEETKDTEAPTAPQNSQLTWKQGRQLLR
QYLQEVGYTDTILDVRSQRVRSLLGLSNSEPNGSVETKNLEQILNGGESPKQKGQEIKRS
SGDVLETFNFLENADDSDEDEENDMIEGIPEGKDKHRMNKHKIGNEGLAADLTDDPDTEE
ALKEFDFLVTAEDGEGAGEARSSGDGTEWAEPITFPSGGGKSFIMGSDDVLLSVLGLGDL
ADLTVTNDADYSYDLPANKDAFRKTWNPKYTLRSHFDGVRALAFHPVEPVLVTASEDHTL
KLWNLQKTVPAKKSASLDVEPIYTFRAHIGPVLSLAISSNGEQCFSGGIDATIQWWNMPS
PSVDPYDTYEPNVLAGTLVGHTDAVWGLAYSGIKNQLLSCSADGTVRLWNPQEKLPCICT
YNGDKKHGIPTSVDFIGCDPAHMVTSFNTGSAVIYDLETSQSLVILSSQVDSGLQSNNHI
NRVVSHPTLPVTITAHEDRHIKFFDNKTGKMIHSMVAHLDAVTSLAVDPNGIYLMSGSHD
CSIRLWNLDSKTCVQEITAHRKKLDESIYDVAFHSSKAYIASAGADALAKVFV
Sequence of entity 3 (C), FASTA
>7K36_3 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C)
MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHG
QFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHES
RQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHI
RALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRA
HQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHV
TRRTPDYFL
Sequence of entity 4 (H), FASTA
>7K36_4 MOB-like protein phocein (chains H)
MVMAEGTAVLRRNRPGTKAQDFYNWPDESFDEMDSTLAVQQYIQQNIRADCSNIDKILEP
PEGQDEGVWKYEHLRQFCLELNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECP
AIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVCRRIYRIFSHAYFHHRQIFDE
YENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGESEA
Sequence of entity 5 (I), FASTA
>7K36_5 Striatin-interacting protein 1 (chains I)
MEPAVGGPGPLIVNNKQPQPPPPPPPAAAQPPPGAPRAAAGLLPGGKAREFNRNQRKDSE
GYSESPDLEFEYADTDKWAAELSELYSYTEGPEFLMNRKCFEEDFRIHVTDKKWTELDTN
QHRTHAMRLLDGLEVTAREKRLKVARAILYVAQGTFGECSSEAEVQSWMRYNIFLLLEVG
TFNALVELLNMEIDNSAACSSAVRKPAISLADSTDLRVLLNIMYLIVETVHQECEGDKAE
WRTMRQTFRAELGSPLYNNEPFAIMLFGMVTKFCSGHAPHFPMKKVLLLLWKTVLCTLGG
FEELQSMKAEKRSILGLPPLPEDSIKVIRNMRAASPPASASDLIEQQQKRGRREHKALIK
QDNLDAFNERDPYKADDSREEEEENDDDNSLEGETFPLERDEVMPPPLQHPQTDRLTCPK
GLPWAPKVREKDIEMFLESSRSKFIGYTLGSDTNTVVGLPRPIHESIKTLKQHKYTSIAE
VQAQMEEEYLRSPLSGGEEEVEQVPAETLYQGLLPSLPQYMIALLKILLAAAPTSKAKTD
SINILADVLPEEMPTTVLQSMKLGVDVNRHKEVIVKAISAVLLLLLKHFKLNHVYQFEYM
AQHLVFANCIPLILKFFNQNIMSYITAKNSISVLDYPHCVVHELPELTAESLEAGDSNQF
CWRNLFSCINLLRILNKLTKWKHSRTMMLVVFKSAPILKRALKVKQAMMQLYVLKLLKVQ
TKYLGRQWRKSNMKTMSAIYQKVRHRLNDDWAYGNDLDARPWDFQAEECALRANIERFNA
RRYDRAHSNPDFLPVDNCLQSVLGQRVDLPEDFQMNYDLWLEREVFSKPISWEELLQ
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MN | Manganese (II) ion | Mn | 2 |
| ZN | Zinc ion | Zn | 2 |
| IHP | Inositol hexakisphosphate | C6 H18 O24 P6 | 1 |
Primary citation
Cryo-EM structure of the Hippo signaling integrator human STRIPAK. Jeong, B.C., Bae, S.J., Ni, L. et al. Nat Struct Mol Biol (2021) 28:290-299. DOI 10.1038/s41594-021-00564-y · 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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