7T0Y: PDB entry 7T0Y

The Ribosomal RNA Processing 1B Protein Phosphatase-1 Holoenzyme. Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Dec 2022.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,081
Mol. weight: 79.9 kDa
Ligands: F, MN
Released: 7 Dec 2022

Explore 7T0Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7T0Y contains 35 α-helices and 38 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	18-21	4
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	169-171	3	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
α-helix	272-274	3
β-strand	280-285	6	2
β-strand	290-298	9	2

Chain B: 3 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	685-686	2	2
α-helix	688-690	3
β-strand	692-696	5	2
α-helix	702-705	4
α-helix	719-721	3
β-strand	726	1	1

Chain C: 17 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
α-helix	56	1
α-helix	58	1
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	121-123	3
α-helix	128-134	7
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	5
β-strand	169-172	4	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	229-239	11
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	290-298	9	6

Chain D: 2 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	685-686	2	6
α-helix	688-690	3
β-strand	692-696	5	6
α-helix	702-704	3
β-strand	726	1	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	A, C	protein	299	Homo sapiens	P62136 (AlphaFold model)
Ribosomal RNA processing protein 1 homolog B	B, D	protein	47	Homo sapiens	Q14684 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>7T0Y_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A, C)
GHMGSLNLDSIIGRLLEVRGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKI
CGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL
RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ
SMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDL
DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD

Sequence of entity 2 (B, D), FASTA

>7T0Y_2 Ribosomal RNA processing protein 1 homolog B (chains B, D)
GKKVTFGLNRNMTAEFKKTDKSILVSPTGPSRVAFDPEQKPLHGVLK

Ligands and cofactors

ID	Name	Formula	Copies
F	Fluoride ion	F	1
MN	Manganese (II) ion	Mn	4

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

Primary citation

The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs. Srivastava, G., Bajaj, R., Kumar, G.S. et al. Cell Rep (2022) 41:111726-111726. DOI 10.1016/j.celrep.2022.111726 · 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)]
6OBS 1.8 Å, PP1 Y134K
6OBQ 1.84 Å, PP1 H66K in complex with Microcystin LR

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