6IUR: A phosphatase complex STRN3-PP2Aa

A phosphatase complex STRN3-PP2Aa. Determined by X-ray diffraction at 3.33 Å resolution. Released 4 Dec 2019.

Method: X-ray diffraction
Resolution: 3.33 Å
Organism: Homo sapiens
Chains: 8
Atoms: 19,541
Mol. weight: 285.39 kDa
Ligands: TME
Released: 4 Dec 2019

Explore 6IUR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6IUR contains 233 α-helices and 0 β-strands across 8 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: 64 helices, 0 β-strands

Element	Residues	Length
α-helix	14-21	8
α-helix	25-33	9
α-helix	35-42	8
α-helix	45-46	2
α-helix	47-51	5
α-helix	52-56	5
α-helix	63-73	11
α-helix	78-80	3
α-helix	83-89	7
α-helix	90-97	8
α-helix	102-116	15
α-helix	121-123	3
α-helix	124-128	5
α-helix	129-136	8
α-helix	141-148	8
α-helix	151-154	4
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	218-226	9
α-helix	228-232	5
α-helix	237-252	16
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	296-304	9
α-helix	307-311	5
α-helix	318-321	4
α-helix	322-326	5
α-helix	327-334	8
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	380-386	7
α-helix	389-395	7
α-helix	397-402	6
α-helix	405-412	8
α-helix	418-422	5
α-helix	427-432	6
α-helix	436-438	3
α-helix	439-443	5
α-helix	444-449	6
α-helix	450-452	3
α-helix	456-473	18
α-helix	475-477	3
α-helix	478-482	5
α-helix	483-489	7
α-helix	495-508	14
α-helix	513-516	4
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

Chain B: 52 helices, 0 β-strands

Element	Residues	Length
α-helix	8-10	3
α-helix	12-20	9
α-helix	26-32	7
α-helix	35-42	8
α-helix	45-46	2
α-helix	47-51	5
α-helix	52-57	6
α-helix	63-73	11
α-helix	78-80	3
α-helix	86-88	3
α-helix	90-96	7
α-helix	102-116	15
α-helix	121-123	3
α-helix	124-128	5
α-helix	129-136	8
α-helix	142-154	13
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	218-234	17
α-helix	237-252	16
α-helix	257-265	9
α-helix	267-274	8
α-helix	277-278	2
α-helix	279-283	5
α-helix	284-291	8
α-helix	296-304	9
α-helix	306-311	6
α-helix	315-321	7
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	389-395	7
α-helix	397-410	14
α-helix	417-434	18
α-helix	444-451	8
α-helix	456-470	15
α-helix	475-477	3
α-helix	478-482	5
α-helix	483-489	7
α-helix	495-508	14
α-helix	514-529	16
α-helix	534-547	14
α-helix	553-566	14
α-helix	573-586	14

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	87-129	43

Chains D and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	89-130	42

Chain E: 54 helices, 0 β-strands

Element	Residues	Length
α-helix	12-20	9
α-helix	26-32	7
α-helix	35-41	7
α-helix	45-46	2
α-helix	47-51	5
α-helix	52-57	6
α-helix	63-73	11
α-helix	78-80	3
α-helix	86-88	3
α-helix	90-96	7
α-helix	102-116	15
α-helix	121-123	3
α-helix	124-128	5
α-helix	129-136	8
α-helix	141-149	9
α-helix	151-154	4
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	218-234	17
α-helix	237-252	16
α-helix	257-265	9
α-helix	268-273	6
α-helix	277-278	2
α-helix	279-283	5
α-helix	284-291	8
α-helix	296-304	9
α-helix	306-311	6
α-helix	315-321	7
α-helix	322-326	5
α-helix	327-333	7
α-helix	341-348	8
α-helix	349-352	4
α-helix	358-360	3
α-helix	361-365	5
α-helix	366-373	8
α-helix	378-386	9
α-helix	389-392	4
α-helix	397-412	16
α-helix	417-434	18
α-helix	440-451	12
α-helix	456-473	18
α-helix	475-478	4
α-helix	483-489	7
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	556-568	13
α-helix	573-586	14

Chain F: 59 helices, 0 β-strands

Element	Residues	Length
α-helix	12-20	9
α-helix	25-33	9
α-helix	36-42	7
α-helix	44-46	3
α-helix	47-51	5
α-helix	52-55	4
α-helix	63-73	11
α-helix	78-80	3
α-helix	83-89	7
α-helix	90-96	7
α-helix	102-116	15
α-helix	121-123	3
α-helix	124-128	5
α-helix	129-136	8
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	206-213	8
α-helix	218-226	9
α-helix	228-232	5
α-helix	237-252	16
α-helix	257-265	9
α-helix	267-273	7
α-helix	275-278	4
α-helix	279-283	5
α-helix	284-291	8
α-helix	296-304	9
α-helix	307-311	5
α-helix	318-321	4
α-helix	322-326	5
α-helix	327-333	7
α-helix	339-346	8
α-helix	358-364	7
α-helix	367-373	7
α-helix	380-386	7
α-helix	390-392	3
α-helix	396-402	7
α-helix	405-412	8
α-helix	417-422	6
α-helix	428-432	5
α-helix	436-442	7
α-helix	444-449	6
α-helix	456-472	17
α-helix	475-477	3
α-helix	478-482	5
α-helix	483-489	7
α-helix	495-508	14
α-helix	513-516	4
α-helix	517-521	5
α-helix	522-529	8
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	573-587	15

Chain G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	86-129	44

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PP2A scaffolding subunit	A, B, E, F	protein	587	Homo sapiens	P30153 (AlphaFold model)
Striatin-3	C, D, G, H	protein	50	Homo sapiens	Q13033 (AlphaFold model)

Sequence of entity 1 (A, B, E, F), FASTA

>6IUR_1 PP2A scaffolding subunit (chains A, B, E, F)
GSPEFDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDE
DEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPS
DLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVR
RAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEA
LVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAA
SHKVKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNTI
EHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLA
IIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATI
IPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAK
SLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA

Sequence of entity 2 (C, D, G, H), FASTA

>6IUR_2 Striatin-3 (chains C, D, G, H)
STMDWEVERAELQARIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAK

Ligands and cofactors

ID	Name	Formula	Copies
TME	Propane	C3 H8	6

Primary citation

Selective Inhibition of STRN3-Containing PP2A Phosphatase Restores Hippo Tumor-Suppressor Activity in Gastric Cancer. Tang, Y., Fang, G., Guo, F. et al. Cancer Cell (2020) 38:115-128.e9. DOI 10.1016/j.ccell.2020.05.019 · 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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