6BQT: 14-3-3 protein theta
Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360. Determined by X-ray diffraction at 2.8 Å resolution. Released 5 Dec 2018.
- Method
- X-ray diffraction
- Resolution
- 2.8 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 15,665
- Mol. weight
- 240.31 kDa
- Ligands
- PE4
- Released
- 5 Dec 2018
Explore 6BQT in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6BQT contains 99 α-helices and 0 β-strands across 9 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: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-16 | 14 | |
| α-helix | 19-31 | 13 | |
| α-helix | 35-36 | 2 | |
| α-helix | 38-67 | 30 | |
| α-helix | 74-100 | 27 | |
| α-helix | 101-105 | 5 | |
| α-helix | 106-108 | 3 | |
| α-helix | 112-130 | 19 | |
| α-helix | 135-159 | 25 | |
| α-helix | 165-180 | 16 | |
| α-helix | 185-201 | 17 | |
| α-helix | 208-229 | 22 | |
Chain B: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-32 | 14 | |
| α-helix | 38-67 | 30 | |
| α-helix | 74-100 | 27 | |
| α-helix | 101-105 | 5 | |
| α-helix | 112-130 | 19 | |
| α-helix | 136-159 | 24 | |
| α-helix | 165-177 | 13 | |
| α-helix | 178-182 | 5 | |
| α-helix | 185-201 | 17 | |
| α-helix | 208-227 | 20 | |
Chain C: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 343-344 | 2 | |
Chain D: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-31 | 13 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-67 | 30 | |
| α-helix | 75-100 | 26 | |
| α-helix | 101-105 | 5 | |
| α-helix | 106-108 | 3 | |
| α-helix | 112-130 | 19 | |
| α-helix | 137-159 | 23 | |
| α-helix | 165-180 | 16 | |
| α-helix | 185-202 | 18 | |
| α-helix | 208-227 | 20 | |
Chain E: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-16 | 14 | |
| α-helix | 19-31 | 13 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-68 | 31 | |
| α-helix | 76-100 | 25 | |
| α-helix | 101-105 | 5 | |
| α-helix | 106-108 | 3 | |
| α-helix | 112-130 | 19 | |
| α-helix | 136-159 | 24 | |
| α-helix | 165-176 | 12 | |
| α-helix | 177-181 | 5 | |
| α-helix | 185-201 | 17 | |
| α-helix | 203-205 | 3 | |
| α-helix | 208-228 | 21 | |
Chain G: 13 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-30 | 12 | |
| α-helix | 35-36 | 2 | |
| α-helix | 38-67 | 30 | |
| α-helix | 76-100 | 25 | |
| α-helix | 101-105 | 5 | |
| α-helix | 112-130 | 19 | |
| α-helix | 136-159 | 24 | |
| α-helix | 165-177 | 13 | |
| α-helix | 178-182 | 5 | |
| α-helix | 185-201 | 17 | |
| α-helix | 203-205 | 3 | |
| α-helix | 208-229 | 22 | |
Chain H: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-16 | 14 | |
| α-helix | 19-30 | 12 | |
| α-helix | 34-36 | 3 | |
| α-helix | 38-68 | 31 | |
| α-helix | 75-100 | 26 | |
| α-helix | 101-105 | 5 | |
| α-helix | 106-108 | 3 | |
| α-helix | 112-132 | 21 | |
| α-helix | 136-159 | 24 | |
| α-helix | 165-180 | 16 | |
| α-helix | 185-202 | 18 | |
| α-helix | 212-229 | 18 | |
Chain J: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-30 | 12 | |
| α-helix | 34-37 | 4 | |
| α-helix | 38-66 | 29 | |
| α-helix | 76-99 | 24 | |
| α-helix | 100-105 | 6 | |
| α-helix | 106-108 | 3 | |
| α-helix | 112-130 | 19 | |
| α-helix | 135-159 | 25 | |
| α-helix | 165-180 | 16 | |
| α-helix | 185-202 | 18 | |
| α-helix | 208-228 | 21 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 14-3-3 protein theta | A, B, D, E, G, H, J, K | protein | 245 | Homo sapiens | P27348 (AlphaFold model) |
| Insulin receptor substrate protein of 53 kDa, peptide (IRSp53) | C, F, I, L | protein | 32 | Homo sapiens | Q9UQB8 (AlphaFold model) |
Sequence of entity 1 (A, B, D, E, G, H, J, K), FASTA
>6BQT_1 14-3-3 protein theta (chains A, B, D, E, G, H, J, K)
MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWR
VISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLK
MKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYE
ILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAA
EGAEN
Sequence of entity 2 (C, F, I, L), FASTA
>6BQT_2 Insulin receptor substrate protein of 53 kDa, peptide (IRSp53) (chains C, F, I, L)
DSYSNTLPVRKSVTPKNSYATTENKTLPRSSS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| PE4 | 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-etha… | C16 H34 O8 | 1 |
Water and common crystallization additives (PEG, PGE, GOL, PG4, EDO, 1PE) are not listed.
Primary citation
Mechanism of IRSp53 inhibition by 14-3-3. Kast, D.J., Dominguez, R. Nat Commun (2019) 10:483-483. DOI 10.1038/s41467-019-08317-8 · 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
- 2BTP 2.8 Å, 14-3-3 Protein Theta (Human) Complexed to Peptide
- 6BD2 2.9 Å, Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366
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