1TCO: Serine/threonine phosphatase B2

Ternary complex of a calcineurin a fragment, calcineurin B, FKBP12 and the immunosuppressant drug FK506 (tacrolimus). Determined by X-ray diffraction at 2.5 Å resolution. Released 12 Feb 1997.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Bos taurus
Chains: 3
Atoms: 5,827
Mol. weight: 75.36 kDa
Ligands: FK5, MYR, CA, PO4
Released: 12 Feb 1997

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

Secondary structure: helices and β-sheets

1TCO contains 31 α-helices and 34 β-strands across 3 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: 18 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	27-28	2
β-strand	29	1	1
α-helix	30	1
α-helix	31-34	4
β-strand	35	1	2
β-strand	41	1	2
α-helix	43-51	9
β-strand	56	1	1
α-helix	58-74	17
β-strand	78-81	4	3
α-helix	82	1
β-strand	85-88	4	4
α-helix	95-105	11
β-strand	113-115	3	4
α-helix	126-139	14
β-strand	144-146	3	4
α-helix	154-159	6
α-helix	162-169	8
α-helix	172-182	11
β-strand	188-191	4	3
β-strand	195-197	3	3
β-strand	203	1	5
β-strand	206	1	5
α-helix	209-213	5
α-helix	221-222	2
α-helix	226-232	7
β-strand	234-235	2	6
β-strand	248-250	3	6
β-strand	258-260	3	6
α-helix	262-272	11
β-strand	276-279	4	3
β-strand	288-290	3	3
β-strand	293	1	7
β-strand	300	1	7
β-strand	302-305	4	3
α-helix	311-313	3
β-strand	319-325	7	4
β-strand	328-334	7	4
α-helix	344-346	3
α-helix	349-369	21

Chain B: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	16-29	14
β-strand	38	1	8
α-helix	39-42	4
α-helix	54-61	8
β-strand	68	1	8
α-helix	71-80	10
α-helix	87-98	12
β-strand	105-106	2	9
α-helix	108-119	12
α-helix	125-139	15
β-strand	147-148	2	9
α-helix	149-156	8
α-helix	161-164	4

Chain C: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2-8	7	10
β-strand	21-30	10	10
β-strand	35-38	4	10
α-helix	39-41	3
β-strand	46-49	4	10
α-helix	57-64	8
β-strand	71-76	6	10
α-helix	78-80	3
β-strand	87	1	11
β-strand	91	1	11
α-helix	92	1
β-strand	97-106	10	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine phosphatase B2	A	protein	375	Bos taurus	P48452 (AlphaFold model)
Serine/threonine phosphatase B2	B	protein	169	Bos taurus	P63099 (AlphaFold model)
FK506-binding protein	C	protein	107	Bos taurus	P18203 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1TCO_1 SERINE/THREONINE PHOSPHATASE B2 (chains A)
VKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEETVALRIITEGASILRQEKN
LLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALK
ILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLC
VHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCS
YFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNN
KAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDEL
GSEEDGFDGATAAAR

Sequence of entity 2 (B), FASTA

>1TCO_2 SERINE/THREONINE PHOSPHATASE B2 (chains B)
GNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDI
FDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVG
NNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV

Sequence of entity 3 (C), FASTA

>1TCO_3 FK506-BINDING PROTEIN (chains C)
GVQVETISPGDGRTFPKAGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWE
EGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE

Ligands and cofactors

ID	Name	Formula	Copies
FK5	8-deethyl-8-[but-3-enyl]-ascomycin	C44 H69 N O12	1
MYR	Myristic acid	C14 H28 O2	1
CA	Calcium ion	Ca	4
PO4	Phosphate ion	O4 P	1
FE	FE (III) ion	Fe	1
ZN	Zinc ion	Zn	1

Primary citation

X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Griffith, J.P., Kim, J.L., Kim, E.E. et al. Cell (1995) 82:507-522. DOI 10.1016/0092-8674(95)90439-5 · PubMed

Other PDB entries of the same protein (UniProt P48452 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2F2O 2.17 Å, Structure of calmodulin bound to a calcineurin peptide: a new way of making an old…
2F2P 2.6 Å, Structure of calmodulin bound to a calcineurin peptide: a new way of making an old…

Browse structure collections

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