6DCX: IASPP-PP-1c structure and targeting of p53

iASPP-PP-1c structure and targeting of p53. Determined by X-ray diffraction at 3.41 Å resolution. Released 15 May 2019.

Method: X-ray diffraction
Resolution: 3.41 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,972
Mol. weight: 126.83 kDa
Released: 15 May 2019

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

Secondary structure: helices and β-sheets

6DCX contains 50 α-helices and 54 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.

Chain A: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	17-21	5
α-helix	23	1
α-helix	32-48	17
β-strand	52-55	4	1
β-strand	59-62	4	2
β-strand	64	1	3
α-helix	69-79	11
β-strand	87-89	3	2
α-helix	100-113	14
β-strand	118-120	3	2
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	1
β-strand	169-172	4	1
α-helix	184-187	4
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	4
β-strand	216-218	3	4
β-strand	225-227	3	4
α-helix	229-239	11
β-strand	243-246	4	1
β-strand	255-258	4	1
β-strand	263-266	4	1
β-strand	267	1	3
α-helix	272-274	3
α-helix	278-279	2
β-strand	280-285	6	2
β-strand	290-296	7	2

Chain B: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	18-21	4
α-helix	23	1
α-helix	32-48	17
β-strand	52-55	4	5
β-strand	59-62	4	6
β-strand	64	1	7
α-helix	69-79	11
β-strand	87-89	3	6
α-helix	100-113	14
β-strand	118-120	3	6
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	5
β-strand	169-172	4	5
α-helix	184-187	4
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	8
β-strand	216-218	3	8
β-strand	225-227	3	8
α-helix	229-238	10
β-strand	243-246	4	5
β-strand	255-258	4	5
β-strand	263-266	4	5
β-strand	267	1	7
α-helix	272-274	3
α-helix	278-279	2
β-strand	280-285	6	6
β-strand	290-296	7	6

Chain C: 10 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	624-625	2	6
α-helix	627-637	11
α-helix	640-649	10
α-helix	663-669	7
α-helix	673-681	9
α-helix	696-702	7
α-helix	706-713	8
α-helix	731-733	3
α-helix	741-754	14
α-helix	759-761	3
β-strand	762-765	4	9
β-strand	769	1	10
β-strand	776	1	9
β-strand	779	1	10
β-strand	784-789	6	9
β-strand	798-803	6	9
β-strand	806-811	6	9
α-helix	812-814	3
β-strand	815-816	2	9

Chain D: 10 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	611	1	1
β-strand	624-625	2	2
α-helix	627-637	11
α-helix	640-649	10
α-helix	663-669	7
α-helix	673-681	9
α-helix	696-702	7
α-helix	706-713	8
β-strand	718	1	11
β-strand	722	1	12
β-strand	729	1	12
α-helix	731-733	3
α-helix	741-754	14
α-helix	758-761	4
β-strand	762-765	4	11
β-strand	769	1	13
β-strand	776	1	11
β-strand	779	1	13
β-strand	784-789	6	11
β-strand	798-803	6	11
β-strand	806-811	6	11
α-helix	812-814	3
β-strand	815-816	2	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	A, B	protein	339	Homo sapiens	P62136 (AlphaFold model)
RelA-associated inhibitor	C, D	protein	228	Homo sapiens	Q8WUF5 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6DCX_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A, B)
GPGYQDPNSMSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPI
LLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYK
IKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFC
CHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEV
VAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMC
SFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK

Sequence of entity 2 (C, D), FASTA

>6DCX_2 RelA-associated inhibitor (chains C, D)
GPGYQDPRSVLRKAGSPRKARRARLNPLVLLLDAALTGELEVVQQAVKEMNDPSQPNEEG
ITALHNAICGANYSIVDFLITAGANVNSPDSHGWTPLHCAASCNDTVICMALVQHGAAIF
ATTLSDGATAFEKCDPYREGYADCATYLADVEQSMGLMNSGAVYALWDYSAEFGDELSFR
EGESVTVLRRDGPEETDWWWAALHGQEGYVPRNYFGLFPRVKPQRSKV

Primary citation

Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Zhou, Y., Millott, R., Kim, H.J. et al. Structure (2019) 27:1485-1496.e4. DOI 10.1016/j.str.2019.07.012 · PubMed

Other PDB entries of the same protein (UniProt P62136 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ZEG 1.09 Å, Structure of PP1-IRSp53 chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)] bound to…
6ZEH 1.3 Å, Structure of PP1-spectrin alpha II chimera [PP1(7-304) + linker (G/S)x9 + spectrin alpha…
6ZEI 1.39 Å, Structure of PP1-IRSp53 S455E chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)]…
6DNO 1.45 Å, Crystal structure of Protein Phosphatase 1 (PP1) bound to the muscle glycogen-targeting…
4MOV 1.45 Å, 1.45 A Resolution Crystal Structure of Protein Phosphatase 1
6OBR 1.5 Å, PP1 Y134A in complex with Microcystin LR
3E7A 1.63 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin Nodularin-R
3E7B 1.7 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin inhibitor Tautomycin
8SW6 1.76 Å, Protein Phosphatase 1 in complex with PP1-specific Phosphatase targeting peptide…
6ZEJ 1.78 Å, Structure of PP1-Phactr1 chimera [PP1(7-304) + linker (SGSGS) + Phactr1(526-580)]
7T0Y 1.8 Å, The Ribosomal RNA Processing 1B Protein Phosphatase-1 Holoenzyme
6OBS 1.8 Å, PP1 Y134K

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