6GHM: PP1 alpha phosphatase

Structure of PP1 alpha phosphatase bound to ASPP2. Determined by X-ray diffraction at 2.15 Å resolution. Released 27 Feb 2019.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,259
Mol. weight: 125.59 kDa
Ligands: MN, NHE
Released: 27 Feb 2019

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

Secondary structure: helices and β-sheets

6GHM contains 49 α-helices and 50 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: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
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	121-123	3
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	1
β-strand	169-172	4	1
α-helix	183-187	5
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
α-helix	318-323	6

Chain B: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
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	169-171	3	5
α-helix	183-187	5
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
β-strand	280-285	6	6
β-strand	290-296	7	6
α-helix	318-323	6

Chain C: 11 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	923-924	2	6
α-helix	926-936	11
α-helix	939-945	7
α-helix	962-968	7
α-helix	972-981	10
α-helix	995-1001	7
α-helix	1005-1012	8
α-helix	1030-1032	3
α-helix	1040-1053	14
α-helix	1057-1060	4
β-strand	1061-1064	4	9
β-strand	1068	1	10
β-strand	1075	1	9
β-strand	1078	1	10
β-strand	1083-1088	6	9
β-strand	1097-1102	6	9
β-strand	1105-1110	6	9
α-helix	1111-1113	3
β-strand	1114-1115	2	9
α-helix	1118-1120	3

Chain D: 12 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	923-924	2	2
α-helix	926-936	11
α-helix	939-945	7
α-helix	946-948	3
α-helix	962-968	7
α-helix	972-981	10
α-helix	995-1001	7
α-helix	1005-1012	8
α-helix	1030-1032	3
α-helix	1040-1053	14
α-helix	1058-1060	3
β-strand	1061-1064	4	11
β-strand	1068	1	12
β-strand	1075	1	11
β-strand	1078	1	12
β-strand	1083-1089	7	11
β-strand	1097-1102	6	11
β-strand	1105-1110	6	11
α-helix	1111-1113	3
β-strand	1114-1115	2	11
α-helix	1118-1121	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	A, B	protein	329	Homo sapiens	P62136 (AlphaFold model)
Apoptosis-stimulating of p53 protein 2	C, D	protein	214	Homo sapiens	Q13625 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6GHM_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A, B)
GHMGSLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKI
CGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL
RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ
SMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDL
DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADK
NKGKYGQFSGLNPGGRPITPPRNSAKAKK

Sequence of entity 2 (C, D), FASTA

>6GHM_2 Apoptosis-stimulating of p53 protein 2 (chains C, D)
GPLGSMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEI
VKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCE
EMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQNDDELPMKEGDCMTIIHREDEDE
IEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	4
NHE	2-[N-cyclohexylamino]ethane sulfonic acid	C8 H17 N O3 S	6

Water and common crystallization additives (GOL, EDO) are not listed.

Primary citation

ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail. Bertran, M.T., Mouilleron, S., Zhou, Y. et al. Nat Commun (2019) 10:771-771. DOI 10.1038/s41467-019-08686-0 · 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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