3N5U: Rb C-terminal peptide

Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1. Determined by X-ray diffraction at 3.2 Å resolution. Released 11 Aug 2010.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,798
Mol. weight: 70.57 kDa
Ligands: MN
Released: 11 Aug 2010

Explore 3N5U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3N5U contains 20 α-helices and 33 β-strands across 3 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: 10 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-53	2	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	199-206	8
β-strand	208-209	2	4
β-strand	216-218	3	4
β-strand	225-227	3	4
α-helix	229-238	10
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	290-296	7	2

Chain B: 10 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-53	2	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	199-206	8
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
β-strand	280-285	6	6
β-strand	291-296	6	6

Chain C: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	876-877	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	A, B	protein	300	Homo sapiens	P62136 (AlphaFold model)
Retinoblastoma-associated protein	C	protein	13	Homo sapiens	P06400 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3N5U_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A, B)
MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD

Sequence of entity 2 (C), FASTA

>3N5U_2 Retinoblastoma-associated protein (chains C)
KPLKKLRFDIEGS

Ligands and cofactors

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

Water and common crystallization additives (CL) are not listed.

Primary citation

An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein. Hirschi, A., Cecchini, M., Steinhardt, R.C. et al. Nat Struct Mol Biol (2010) 17:1051-1057. DOI 10.1038/nsmb.1868 · 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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