2BTP: 14-3-3 protein tau

14-3-3 Protein Theta (Human) Complexed to Peptide. Determined by X-ray diffraction at 2.8 Å resolution. Released 28 Jun 2005.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 3,727
Mol. weight: 60.06 kDa
Released: 28 Jun 2005

Explore 2BTP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BTP contains 26 α-helices and 2 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: 13 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	-16	1	1
β-strand	-10	1	1
α-helix	-4--1	4
α-helix	3-15	13
α-helix	19-31	13
α-helix	34-36	3
α-helix	38-68	31
α-helix	75-100	26
α-helix	101-105	5
α-helix	112-132	21
α-helix	135-159	25
α-helix	165-176	12
α-helix	177-182	6
α-helix	185-201	17
α-helix	208-227	20

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-31	13
α-helix	35-36	2
α-helix	38-67	30
α-helix	75-100	26
α-helix	101-105	5
α-helix	112-130	19
α-helix	135-159	25
α-helix	165-176	12
α-helix	177-182	6
α-helix	185-201	17
α-helix	202-204	3
α-helix	211-227	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein tau	A, B	protein	256	HOMO SAPIENS	P27348 (AlphaFold model)
Consensus peptide for 14-3-3 proteins	P, Q	protein	6	HOMO SAPIENS

Sequence of entity 1 (A, B), FASTA

>2BTP_1 14-3-3 PROTEIN TAU (chains A, B)
MHHHHHHSSGVDLGTENLYFQSMEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSN
EERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVL
ELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKK
EMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIM
QLLRDNLTLWTSDSAG

Sequence of entity 2 (P, Q), FASTA

>2BTP_2 CONSENSUS PEPTIDE FOR 14-3-3 PROTEINS (chains P, Q)
RQRSAP

Primary citation

Structural Basis for Protein-Protein Interactions in the 14-3-3 Protein Family. Yang, X., Lee, W.H., Sobott, F. et al. Proc Natl Acad Sci U S A (2006) 103:17237. DOI 10.1073/PNAS.0605779103 · PubMed

Other PDB entries of the same protein (UniProt P27348 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6BCR 1.99 Å, Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at T340
6KZG 2.0 Å, 14-3-3 protein in Complex with CIC S301 phosphorylated peptide
6BCY 2.3 Å, Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at T360
6BD1 2.35 Å, Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at S366
5IQP 2.6 Å, 14-3-3 protein tau isoform
6KZH 2.65 Å, 14-3-3 protein in Complex with CIC S173 phosphorylated peptide
6BQT 2.8 Å, Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360
6BD2 2.9 Å, Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366

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