1U32: Protein Phosphatase-1: Calcineurin Hybrid

Crystal structure of a Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid. Determined by X-ray diffraction at 2.0 Å resolution. Released 17 Aug 2004.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,531
Mol. weight: 34.92 kDa
Ligands: OKA, MN
Released: 17 Aug 2004

Explore 1U32 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1U32 contains 12 α-helices and 16 β-strands across 1 chain. 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: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	23	1
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	200-206	7
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
α-helix	272-274	3
β-strand	280-285	6	2
β-strand	291-296	6	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine protein phosphatase PP1-gamma catalytic subunit	A	protein	293	Homo sapiens	P36873 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1U32_1 Serine/threonine protein phosphatase PP1-gamma catalytic subunit (chains A)
KLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDI
HGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNH
ECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQ
IRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLIC
RAHQVVEDGYEFFAKRQLVTLFSAPNYLDVYNNAGAMMSVDETLMCSFQILKP

Ligands and cofactors

ID	Name	Formula	Copies
OKA	Okadaic acid	C44 H68 O13	1
MN	Manganese (II) ion	Mn	2

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

Primary citation

Crystal Structure and Mutagenesis of a Protein Phosphatase-1:Calcineurin Hybrid Elucidate the Role of the {beta}12-{beta}13 Loop in Inhibitor Binding. Maynes, J.T., Perreault, K.R., Cherney, M.M. et al. J Biol Chem (2004) 279:43198-43206. DOI 10.1074/jbc.M407184200 · PubMed

Other PDB entries of the same protein (UniProt P36873 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5INB 1.3 Å, RepoMan-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex
1JK7 1.9 Å, Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1
4UT2 1.96 Å, X-ray structure of the human PP1 gamma catalytic subunit treated with ascorbate
1IT6 2.0 Å, Crystal structure of the complex between calyculin a and the catalytic subunit of…
5J28 2.0 Å, Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex
2BCD 2.1 Å, X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound
4UT3 2.19 Å, X-ray structure of the human PP1 gamma catalytic subunit treated with hydrogen peroxide
2BDX 2.3 Å, X-ray Crystal Structure of dihydromicrocystin-LA bound to Protein Phosphatase-1
7SD0 2.95 Å, Cryo-EM structure of the SHOC2:PP1C:MRAS complex
8B5R 6.1 Å, p97-p37-SPI substrate complex

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