Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366. Determined by X-ray diffraction at 2.9 Å resolution. Released 24 Oct 2018.
Explore 6BD2 in 3D Show helices and sheets RCSB PDB PDBe
6BD2 contains 26 α-helices and 0 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-16 | 13 | |
| α-helix | 19-32 | 14 | |
| α-helix | 35-36 | 2 | |
| α-helix | 38-67 | 30 | |
| α-helix | 76-100 | 25 | |
| α-helix | 101-105 | 5 | |
| α-helix | 106-108 | 3 | |
| α-helix | 112-130 | 19 | |
| α-helix | 135-159 | 25 | |
| α-helix | 165-176 | 12 | |
| α-helix | 177-181 | 5 | |
| α-helix | 185-201 | 17 | |
| α-helix | 203-205 | 3 | |
| α-helix | 211-228 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-31 | 13 | |
| α-helix | 34-37 | 4 | |
| α-helix | 38-66 | 29 | |
| α-helix | 73-100 | 28 | |
| α-helix | 101-105 | 5 | |
| α-helix | 112-130 | 19 | |
| α-helix | 135-159 | 25 | |
| α-helix | 165-180 | 16 | |
| α-helix | 185-201 | 17 | |
| α-helix | 211-227 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 337-339 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein theta | A, B | protein | 245 | Homo sapiens | P27348 (AlphaFold model) |
| Insulin receptor substrate protein of 53 kDa, peptide (IRSp53) | C | protein | 38 | Homo sapiens | Q9UQB8 (AlphaFold model) |
>6BD2_1 14-3-3 protein theta (chains A, B) MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWR VISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLK MKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYE ILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAA EGAEN
>6BD2_2 Insulin receptor substrate protein of 53 kDa, peptide (IRSp53) (chains C) DSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLE
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:
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