6DNO: Protein Phosphatase 1

Crystal structure of Protein Phosphatase 1 (PP1) bound to the muscle glycogen-targeting subunit (Gm). Determined by X-ray diffraction at 1.45 Å resolution. Released 23 Jan 2019.

Method: X-ray diffraction
Resolution: 1.45 Å
Organisms: Homo sapiens, Oryctolagus cuniculus, synthetic construct
Chains: 3
Atoms: 2,781
Mol. weight: 38.63 kDa
Released: 23 Jan 2019

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

Secondary structure: helices and β-sheets

6DNO contains 14 α-helices and 18 β-strands across 2 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	9-16	8
α-helix	17-19	3
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	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	183-187	5
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
β-strand	280-285	6	2
β-strand	290-298	9	2

Chain B: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	67-68	2	2
α-helix	69-72	4
β-strand	77-82	6	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	A	protein	299	Homo sapiens	P62136 (AlphaFold model)
Protein phosphatase 1 regulatory subunit 3A	B	protein	30	Oryctolagus cuniculus	Q00756 (AlphaFold model)
Microcystin-LR	C	protein	7	synthetic construct

Sequence of entity 1 (A), FASTA

>6DNO_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A)
GHMGSLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKI
CGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL
RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ
SMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDL
DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD

Sequence of entity 2 (B), FASTA

>6DNO_2 Protein phosphatase 1 regulatory subunit 3A (chains B)
RRVSFADNFGFNLVSVKEFDTWELPSVSTT

Sequence of entity 3 (C), FASTA

>6DNO_3 Microcystin-LR (chains C)
ALDRXEX

Primary citation

Identification of the substrate recruitment mechanism of the muscle glycogen protein phosphatase 1 holoenzyme. Kumar, G.S., Choy, M.S., Koveal, D.M. et al. Sci Adv (2018) 4:eaau6044-eaau6044. DOI 10.1126/sciadv.aau6044 · 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)]…
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
6OBQ 1.84 Å, PP1 H66K in complex with Microcystin LR

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