1IT6: PDB entry 1IT6

Crystal structure of the complex between calyculin a and the catalytic subunit of protein phosphatase 1. Determined by X-ray diffraction at 2.0 Å resolution. Released 22 May 2002.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,936
Mol. weight: 76.3 kDa
Ligands: MN, CYU
Released: 22 May 2002

Explore 1IT6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1IT6 contains 24 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	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	1
β-strand	169-172	4	1
α-helix	183-187	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	229-239	11
β-strand	243-246	4	1
β-strand	255-258	4	1
β-strand	263-266	4	1
β-strand	267	1	3
α-helix	272-274	3
β-strand	280-285	6	2
β-strand	291-296	6	2

Chain B: 13 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	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	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	5
β-strand	169-172	4	5
α-helix	183-187	5
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
α-helix	272-274	3
β-strand	280-285	6	6
β-strand	291-296	6	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine protein phosphatase 1 gamma (PP1-gamma) catalytic subunit	A, B	protein	323	Homo sapiens	P36873 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1IT6_1 SERINE/THREONINE PROTEIN PHOSPHATASE 1 GAMMA (PP1-GAMMA) CATALYTIC SUBUNIT (chains A, B)
MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE
KKKPNATRPVTPPRGMITKQAKK

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	4
CYU	Calyculin a	C50 H81 N4 O15 P	2

Primary citation

Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1. Kita, A., Matsunaga, S., Takai, A. et al. Structure (2002) 10:715-724. DOI 10.1016/S0969-2126(02)00764-5 · 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
1U32 2.0 Å, Crystal structure of a Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid
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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