1S95: Serine/threonine protein phosphatase 5

Structure of serine/threonine protein phosphatase 5. Determined by X-ray diffraction at 1.6 Å resolution. Released 24 Aug 2004.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,748
Mol. weight: 76.42 kDa
Ligands: PO4, MN
Released: 24 Aug 2004

Explore 1S95 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1S95 contains 28 α-helices and 36 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: 14 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	182	1	1
β-strand	185	1	1
α-helix	188-199	12
α-helix	206-221	16
β-strand	226-229	4	2
β-strand	236-240	5	3
α-helix	247-257	11
β-strand	261	1	4
β-strand	264	1	4
β-strand	266-269	4	3
α-helix	279-292	14
β-strand	297-300	4	3
α-helix	307-313	7
α-helix	315-322	8
α-helix	325-335	11
β-strand	341-344	4	2
β-strand	348-350	3	2
α-helix	363-367	5
α-helix	375-376	2
α-helix	380-386	7
β-strand	388-389	2	5
β-strand	395-397	3	5
β-strand	404-406	3	5
α-helix	408-418	11
β-strand	422-425	4	2
β-strand	434-437	4	2
α-helix	438-440	3
β-strand	442-445	4	2
α-helix	451-453	3
β-strand	459-465	7	3
β-strand	468-476	9	3
α-helix	492-495	4

Chain B: 14 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	182	1	6
β-strand	185	1	6
α-helix	188-199	12
α-helix	206-221	16
β-strand	226-229	4	7
β-strand	236-240	5	8
α-helix	247-257	11
β-strand	261	1	9
β-strand	264	1	9
β-strand	266-269	4	8
α-helix	279-292	14
β-strand	297-300	4	8
α-helix	307-313	7
α-helix	315-322	8
α-helix	325-335	11
β-strand	341-344	4	7
β-strand	348-350	3	7
α-helix	363-367	5
α-helix	374-376	3
α-helix	380-386	7
β-strand	388-389	2	10
β-strand	395-397	3	10
β-strand	404-406	3	10
α-helix	408-418	11
β-strand	422-425	4	7
β-strand	434-437	4	7
α-helix	438-440	3
β-strand	442-445	4	7
α-helix	451-453	3
β-strand	459-465	7	8
β-strand	470-476	7	8
α-helix	492-497	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine protein phosphatase 5	A, B	protein	333	Homo sapiens	P53041 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1S95_1 Serine/threonine protein phosphatase 5 (chains A, B)
GASMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTL
VETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTL
FGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCING
KVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQF
GPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQG
SDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2
MN	Manganese (II) ion	Mn	4

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

Primary citation

Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5. Swingle, M.R., Honkanen, R.E., Ciszak, E.M. J Biol Chem (2004) 279:33992-33999. DOI 10.1074/jbc.M402855200 · PubMed

Other PDB entries of the same protein (UniProt P53041 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ZX2 1.23 Å, Co-crystal structures of PP5 in complex with 5-methyl-7-oxabicyclo[2.2.1]heptane-2,3-dica…
3H63 1.3 Å, Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms…
3H62 1.4 Å, Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms…
3H61 1.45 Å, Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms…
3H68 1.5 Å, Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Zn2+ atoms…
3H67 1.65 Å, Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Zn2+ atoms…
5WG8 1.65 Å, Structure of PP5C with LB-100; 7-oxabicyclo[2.2.1]heptane-2,3-dicarbonyl moiety modeled…
3H64 1.9 Å, Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms…
5UI1 1.96 Å, Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole…
3H60 2.0 Å, Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Mn2+ atoms
4ZVZ 2.0 Å, Co-crystal structures of PP5 in complex with 5-methyl-7-oxabicyclo[2.2.1]heptane-2,3-dica…
3H69 2.1 Å, Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms…

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