1FJM: Protein serine/threonine phosphatase-1

Protein serine/threonine phosphatase-1 (alpha isoform, type 1) complexed with microcystin-LR toxin. Determined by X-ray diffraction at 2.1 Å resolution. Released 20 Jun 1996.

Method: X-ray diffraction
Resolution: 2.1 Å
Organisms: Oryctolagus cuniculus, Microcystis aeruginosa
Chains: 4
Atoms: 5,004
Mol. weight: 77.52 kDa
Ligands: MN
Released: 20 Jun 1996

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

Secondary structure: helices and β-sheets

1FJM contains 22 α-helices and 32 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: 11 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-18	10
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	128-134	7
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	1
β-strand	169-172	4	1
α-helix	183-188	6
α-helix	194-196	3
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	229-239	11
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	291-296	6	2

Chain B: 11 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-18	10
α-helix	32-48	17
β-strand	52-55	4	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	128-133	6
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	5
β-strand	169-172	4	5
α-helix	184-187	4
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	8
β-strand	216-218	3	8
β-strand	225-227	3	8
α-helix	229-239	11
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein serine/threonine phosphatase-1 (alpha isoform, type 1)	A, B	protein	330	Oryctolagus cuniculus	P62139 (AlphaFold model)
microcystin LR	M, N	protein	7	Microcystis aeruginosa

Sequence of entity 1 (A, B), FASTA

>1FJM_1 PROTEIN SERINE/THREONINE PHOSPHATASE-1 (ALPHA ISOFORM, TYPE 1) (chains A, B)
MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
KNKGKYGQFSGLNPGGRPITPPRNSAKAKK

Sequence of entity 2 (M, N), FASTA

>1FJM_2 microcystin LR (chains M, N)
ALDRXEX

Ligands and cofactors

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

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

Primary citation

Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Goldberg, J., Huang, H.B., Kwon, Y.G. et al. Nature (1995) 376:745-753. DOI 10.1038/376745a0 · PubMed

Other PDB entries of the same protein (UniProt P62139 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7NZM 3.96 Å, Cryo-EM structure of pre-dephosphorylation complex of phosphorylated eIF2alpha with…

Browse structure collections

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