6ZEJ: PDB entry 6ZEJ

Structure of PP1-Phactr1 chimera [PP1(7-304) + linker (SGSGS) + Phactr1(526-580)]. Determined by X-ray diffraction at 1.78 Å resolution. Released 30 Sept 2020.

Method: X-ray diffraction
Resolution: 1.78 Å
Organism: Homo sapiens
Chains: 6
Atoms: 17,414
Mol. weight: 250.36 kDa
Ligands: MN
Released: 30 Sept 2020

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

Secondary structure: helices and β-sheets

6ZEJ contains 112 α-helices and 102 β-strands across 6 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: 20 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	8-16	9
α-helix	22	1
α-helix	25-27	3
α-helix	31-47	17
β-strand	51-54	4	5
β-strand	58-61	4	6
β-strand	63	1	7
α-helix	68-78	11
β-strand	86-88	3	6
α-helix	99-112	14
β-strand	117-119	3	6
α-helix	120-122	3
α-helix	127-130	4
α-helix	135-142	8
α-helix	145-155	11
β-strand	161-164	4	5
β-strand	168-170	3	5
α-helix	182-186	5
α-helix	193-195	3
α-helix	199-205	7
β-strand	207-208	2	8
β-strand	215-217	3	8
β-strand	224-226	3	8
α-helix	228-237	10
β-strand	242-245	4	5
β-strand	254-257	4	5
β-strand	262-265	4	5
β-strand	266	1	7
α-helix	271-273	3
α-helix	277-278	2
β-strand	279-284	6	6
β-strand	290-296	7	6
β-strand	310-314	5	6
α-helix	315-316	2
α-helix	325-328	4
α-helix	331-347	17
α-helix	353-358	6

Chain D: 19 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	8-16	9
α-helix	25-27	3
α-helix	31-47	17
β-strand	51-54	4	1
β-strand	58-61	4	2
β-strand	63	1	3
α-helix	68-78	11
β-strand	86-88	3	2
α-helix	99-112	14
β-strand	117-119	3	2
α-helix	120-122	3
α-helix	127-130	4
α-helix	135-142	8
α-helix	145-155	11
β-strand	161-164	4	1
β-strand	168-170	3	1
α-helix	182-186	5
α-helix	193-195	3
α-helix	199-205	7
β-strand	207-208	2	4
β-strand	215-217	3	4
β-strand	224-226	3	4
α-helix	228-238	11
β-strand	242-245	4	1
β-strand	254-257	4	1
β-strand	262-265	4	1
β-strand	266	1	3
α-helix	271-273	3
α-helix	277-278	2
β-strand	279-284	6	2
β-strand	290-296	7	2
β-strand	311-314	4	2
α-helix	315-316	2
α-helix	325-328	4
α-helix	331-347	17
α-helix	353-358	6

Chain F: 17 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	8-16	9
α-helix	31-47	17
β-strand	51-54	4	9
β-strand	58-61	4	10
β-strand	63	1	11
α-helix	68-78	11
β-strand	86-88	3	10
α-helix	99-112	14
β-strand	117-119	3	10
α-helix	127-130	4
α-helix	135-142	8
α-helix	145-155	11
β-strand	161-164	4	9
β-strand	168-170	3	9
α-helix	183-186	4
α-helix	199-205	7
β-strand	207-208	2	12
β-strand	215-217	3	12
β-strand	224-226	3	12
α-helix	228-238	11
β-strand	242-245	4	9
β-strand	254-257	4	9
β-strand	262-265	4	9
β-strand	266	1	11
α-helix	271-273	3
α-helix	277-278	2
β-strand	279-284	6	10
β-strand	290-296	7	10
β-strand	311-314	4	10
α-helix	315-316	2
α-helix	325-328	4
α-helix	331-343	13
α-helix	344-348	5
α-helix	353-358	6

Chain I: 19 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	8-16	9
α-helix	22	1
α-helix	31-47	17
β-strand	51-54	4	13
β-strand	58-61	4	14
β-strand	63	1	15
α-helix	68-78	11
β-strand	86-88	3	14
α-helix	99-112	14
β-strand	117-119	3	14
α-helix	120-122	3
α-helix	127-130	4
α-helix	135-142	8
α-helix	145-155	11
β-strand	161-164	4	13
β-strand	168-170	3	13
α-helix	182-186	5
α-helix	193-195	3
α-helix	199-205	7
β-strand	207-208	2	16
β-strand	215-217	3	16
β-strand	224-226	3	16
α-helix	228-237	10
β-strand	242-245	4	13
β-strand	254-257	4	13
β-strand	262-265	4	13
β-strand	266	1	15
α-helix	271-273	3
α-helix	277-278	2
β-strand	279-284	6	14
β-strand	290-296	7	14
β-strand	311-314	4	14
α-helix	315-316	2
α-helix	325-328	4
α-helix	331-347	17
α-helix	353-358	6

Chain L: 18 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	8-17	10
α-helix	25-27	3
α-helix	31-47	17
β-strand	51-54	4	17
β-strand	58-61	4	18
β-strand	63	1	19
α-helix	68-78	11
β-strand	86-88	3	18
α-helix	99-112	14
β-strand	117-119	3	18
α-helix	120-122	3
α-helix	127-130	4
α-helix	135-142	8
α-helix	145-155	11
β-strand	161-164	4	17
β-strand	168-171	4	17
α-helix	183-186	4
α-helix	193-195	3
α-helix	199-205	7
β-strand	207-208	2	20
β-strand	215-217	3	20
β-strand	224-226	3	20
α-helix	228-237	10
β-strand	242-245	4	17
β-strand	254-257	4	17
β-strand	262-265	4	17
β-strand	266	1	19
α-helix	271-273	3
β-strand	279-284	6	18
β-strand	290-297	8	18
β-strand	311-315	5	18
α-helix	316	1
α-helix	325-328	4
α-helix	331-347	17
α-helix	353-358	6

Chain O: 19 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	8-16	9
α-helix	25-27	3
α-helix	31-47	17
β-strand	51-54	4	21
β-strand	58-61	4	22
β-strand	63	1	23
α-helix	68-78	11
β-strand	86-88	3	22
α-helix	99-112	14
β-strand	117-119	3	22
α-helix	127-130	4
α-helix	135-142	8
α-helix	145-155	11
β-strand	161-164	4	21
β-strand	168-170	3	21
α-helix	182-186	5
α-helix	193-195	3
α-helix	199-205	7
β-strand	207-208	2	24
β-strand	215-217	3	24
β-strand	224-226	3	24
α-helix	228-238	11
β-strand	242-245	4	21
β-strand	254-257	4	21
β-strand	262-265	4	21
β-strand	266	1	23
α-helix	271-273	3
α-helix	277-278	2
β-strand	279-284	6	22
β-strand	290-296	7	22
β-strand	310-314	5	22
α-helix	315-316	2
α-helix	325-328	4
α-helix	331-343	13
α-helix	344-348	5
α-helix	353-358	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit,Phosphatase and actin regulator	A, D, F, I, L, O	protein	363	Homo sapiens	P62136 (AlphaFold model), Q9C0D0 (AlphaFold model)

Sequence of entity 1 (A, D, F, I, L, O), FASTA

>6ZEJ_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit,Phosphatase and actin regulator (chains A, D, F, I, L, O)
GHMGSLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKI
CGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL
RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ
SMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDL
DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADK
NKGSGSGSVEVADAQDYDRRADKPWTRLTAADKAAIRKELNEFKSTEMEVHELSRHLTRF
HRP

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	12

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

Primary citation

Molecular basis for substrate specificity of the Phactr1/PP1 phosphatase holoenzyme. Fedoryshchak, R.O., Prechova, M., Butler, A. et al. Elife (2020) 9. DOI 10.7554/eLife.61509 · 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…
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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