5UI1: Human Protein Phosphatase 5C

Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole inhibitor. Determined by X-ray diffraction at 1.96 Å resolution. Released 17 Jan 2018.

Method: X-ray diffraction
Resolution: 1.96 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,491
Mol. weight: 152.74 kDa
Ligands: 8D4, MN
Released: 17 Jan 2018

Explore 5UI1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5UI1 contains 53 α-helices and 78 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: 14 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	188-199	12
α-helix	202-205	4
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	325-335	11
β-strand	341-344	4	1
β-strand	348-351	4	1
α-helix	363-368	6
α-helix	374-376	3
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	408-417	10
β-strand	422-425	4	1
β-strand	434-437	4	1
α-helix	438-440	3
β-strand	442-445	4	1
β-strand	446	1	3
α-helix	451-453	3
β-strand	459-465	7	2
β-strand	472-476	5	2

Chain B: 13 helices, 20 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
β-strand	242	1	9
α-helix	247-257	11
β-strand	261	1	10
β-strand	264	1	10
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	325-336	12
β-strand	341-344	4	7
β-strand	348-351	4	7
α-helix	363-367	5
α-helix	374-376	3
α-helix	380-386	7
β-strand	388-389	2	11
β-strand	395-397	3	11
β-strand	404-406	3	11
α-helix	408-417	10
β-strand	422-425	4	7
β-strand	434-437	4	7
α-helix	438-440	3
β-strand	442-445	4	7
β-strand	446	1	9
α-helix	451-453	3
β-strand	459-465	7	8
β-strand	472-476	5	8

Chain C: 12 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	182	1	12
β-strand	185	1	12
α-helix	188-199	12
α-helix	206-221	16
β-strand	226-229	4	13
β-strand	236-240	5	14
β-strand	242	1	15
α-helix	247-257	11
β-strand	261	1	16
β-strand	264	1	16
β-strand	266-269	4	14
α-helix	279-292	14
β-strand	297-300	4	14
α-helix	307-313	7
α-helix	315-322	8
α-helix	325-335	11
β-strand	341-344	4	13
β-strand	348-351	4	13
α-helix	363-367	5
α-helix	374-376	3
α-helix	380-386	7
β-strand	388-389	2	17
β-strand	395-397	3	17
β-strand	404-406	3	17
α-helix	408-417	10
β-strand	422-425	4	13
β-strand	434-437	4	13
β-strand	442-445	4	13
β-strand	446	1	15
α-helix	451-453	3
β-strand	459-465	7	14
β-strand	471-476	6	14

Chain D: 14 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	182	1	18
β-strand	185	1	18
α-helix	188-199	12
α-helix	203-205	3
α-helix	206-221	16
β-strand	226-229	4	19
β-strand	236-240	5	20
β-strand	242	1	21
α-helix	247-257	11
β-strand	261	1	22
β-strand	264	1	22
β-strand	266-269	4	20
α-helix	279-292	14
β-strand	297-300	4	20
α-helix	307-312	6
α-helix	315-322	8
α-helix	325-335	11
β-strand	341-344	4	19
β-strand	348-351	4	19
α-helix	363-368	6
α-helix	375-376	2
α-helix	380-386	7
β-strand	388-389	2	23
β-strand	395-397	3	23
β-strand	404-406	3	23
α-helix	408-418	11
β-strand	422-425	4	19
β-strand	434-437	4	19
α-helix	438-440	3
β-strand	442-445	4	19
β-strand	446	1	21
α-helix	451-453	3
β-strand	459-465	7	20
β-strand	468-476	9	20

Molecules and chains

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

Sequence of entity 1 (A, B, C, D), FASTA

>5UI1_1 Serine/threonine-protein phosphatase 5 (chains A, B, C, D)
GASMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTL
VETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTL
FGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCING
KVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQF
GPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQG
SDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM

Ligands and cofactors

ID	Name	Formula	Copies
8D4	5-phenyl-1H-1,2,3-triazole-4-carboxylic acid	C9 H7 N3 O2	4
MN	Manganese (II) ion	Mn	8

Primary citation

Crystal Structure Human PP5C in Complex with an Inhibitor. Chattopadhyay, D., Swingle, M.R., Salter, E.A. et al. To be published.

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…
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…

Browse structure collections

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