1WAO: PP5 structure

PP5 structure. Determined by X-ray diffraction at 2.9 Å resolution. Released 22 Feb 2005.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 15,082
Mol. weight: 218.71 kDa
Ligands: MN
Released: 22 Feb 2005

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

Secondary structure: helices and β-sheets

1WAO contains 85 α-helices and 69 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 1: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	25-28	4
α-helix	44-57	14
α-helix	62-74	13
α-helix	78-90	13
α-helix	96-109	14
α-helix	112-125	14
α-helix	132-148	17
α-helix	182-184	3
α-helix	188-199	12
α-helix	203-205	3
α-helix	206-221	16
β-strand	226-229	4	1
β-strand	236-240	5	2
β-strand	242	1	3
α-helix	247-257	11
β-strand	261	1	4
β-strand	264	1	4
β-strand	266-269	4	2
α-helix	279-292	14
β-strand	297-300	4	2
α-helix	307-313	7
α-helix	315-322	8
α-helix	327-335	9
β-strand	341-344	4	1
β-strand	348-350	3	1
α-helix	363-367	5
α-helix	374-376	3
α-helix	380-386	7
β-strand	388-389	2	5
β-strand	396-397	2	5
β-strand	404-406	3	5
α-helix	408-417	10
β-strand	422-425	4	1
β-strand	432-433	2	2
β-strand	434-437	4	1
α-helix	438-440	3
β-strand	442-445	4	1
β-strand	446	1	3
β-strand	458-465	8	2
β-strand	468-476	9	2
α-helix	492-495	4

Chain 2: 20 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	26-40	15
α-helix	44-57	14
α-helix	62-74	13
α-helix	78-90	13
α-helix	96-109	14
α-helix	112-125	14
α-helix	132-148	17
α-helix	188-199	12
α-helix	203-205	3
α-helix	206-221	16
β-strand	226-229	4	6
β-strand	236-240	5	7
β-strand	242	1	8
α-helix	247-256	10
β-strand	266-268	3	7
α-helix	279-292	14
β-strand	297-299	3	7
α-helix	307-313	7
α-helix	315-322	8
α-helix	327-335	9
β-strand	341-344	4	6
β-strand	348-350	3	6
α-helix	363-367	5
α-helix	374-376	3
α-helix	380-386	7
β-strand	388-389	2	9
β-strand	396-397	2	9
β-strand	404-406	3	9
α-helix	408-417	10
β-strand	422-425	4	6
β-strand	434-437	4	6
α-helix	438-440	3
β-strand	442-445	4	6
β-strand	446	1	8
β-strand	459-465	7	7
β-strand	468-476	9	7

Chain 3: 23 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	29-31	3
α-helix	36-41	6
α-helix	45-49	5
α-helix	64-71	8
α-helix	78-84	7
α-helix	96-108	13
α-helix	114-120	7
α-helix	134-143	10
α-helix	145-148	4
α-helix	182-184	3
α-helix	188-199	12
α-helix	203-205	3
α-helix	206-221	16
β-strand	226-229	4	10
β-strand	236-240	5	11
β-strand	242	1	12
α-helix	247-256	10
β-strand	266-268	3	11
α-helix	279-292	14
β-strand	297-299	3	11
α-helix	307-313	7
α-helix	315-322	8
α-helix	327-335	9
β-strand	341-344	4	10
β-strand	348-350	3	10
α-helix	363-367	5
α-helix	374-376	3
α-helix	380-386	7
β-strand	388-389	2	13
β-strand	396-397	2	13
β-strand	404-406	3	13
α-helix	408-417	10
β-strand	422-425	4	10
β-strand	432	1	14
β-strand	434-437	4	10
α-helix	438-440	3
β-strand	442-445	4	10
β-strand	446	1	12
β-strand	458	1	14
β-strand	459-465	7	11
β-strand	472-476	5	11

Chain 4: 20 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	27-40	14
α-helix	44-57	14
α-helix	62-74	13
α-helix	78-90	13
α-helix	96-109	14
α-helix	112-125	14
α-helix	132-148	17
α-helix	188-199	12
α-helix	203-205	3
α-helix	206-221	16
β-strand	226-229	4	15
β-strand	236-240	5	16
α-helix	247-257	11
β-strand	261	1	17
β-strand	264	1	17
β-strand	266-268	3	16
α-helix	279-292	14
β-strand	297-299	3	16
α-helix	307-313	7
α-helix	315-322	8
α-helix	327-335	9
β-strand	341-344	4	15
β-strand	348-350	3	15
α-helix	363-367	5
α-helix	374-376	3
α-helix	380-386	7
β-strand	388-389	2	18
β-strand	396-397	2	18
β-strand	404-406	3	18
α-helix	408-417	10
β-strand	422-425	4	15
β-strand	434-437	4	15
α-helix	438-440	3
β-strand	442-445	4	15
β-strand	459-465	7	16
β-strand	468-476	9	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine protein phosphatase 5	1, 2, 3, 4	protein	477	HOMO SAPIENS	P53041 (AlphaFold model)

Sequence of entity 1 (1, 2, 3, 4), FASTA

>1WAO_1 SERINE/THREONINE PROTEIN PHOSPHATASE 5 (chains 1, 2, 3, 4)
GALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYAL
GDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKI
VKQKAFERAIAGDEHKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQK
KLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSE
TNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAK
YTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMC
DLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRC
VTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	8

Primary citation

Molecular Basis for Tpr Domain-Mediated Regulation of Protein Phosphatase 5. Yang, J., Roe, S.M., Cliff, M.J. et al. EMBO J (2005) 24:1. DOI 10.1038/SJ.EMBOJ.7600496 · 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…
1S95 1.6 Å, Structure of serine/threonine protein phosphatase 5
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…

Browse structure collections

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