14-3-3 protein zeta bound to R18 peptide. Determined by X-ray diffraction at 3.35 Å resolution. Released 2 Mar 1999.
Explore 1A38 in 3D Show helices and sheets RCSB PDB PDBe
1A38 contains 24 α-helices and 0 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-14 | 12 | |
| α-helix | 19-30 | 12 | |
| α-helix | 38-66 | 29 | |
| α-helix | 74-100 | 27 | |
| α-helix | 101-105 | 5 | |
| α-helix | 106-108 | 3 | |
| α-helix | 112-131 | 20 | |
| α-helix | 136-157 | 22 | |
| α-helix | 167-176 | 10 | |
| α-helix | 177-182 | 6 | |
| α-helix | 185-201 | 17 | |
| α-helix | 212-225 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein zeta | A, B | protein | 245 | Bos taurus | P63103 (AlphaFold model) |
| R18 peptide (phcvprdlswldleanmclp) | P, Q | protein | 20 |
>1A38_1 14-3-3 PROTEIN ZETA (chains A, B) MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWR VVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK MKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYE ILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAG EGGEN
>1A38_2 R18 PEPTIDE (PHCVPRDLSWLDLEANMCLP) (chains P, Q) FHCVPRDLSWLDLEANMCLP
14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. Petosa, C., Masters, S.C., Bankston, L.A. et al. J Biol Chem (1998) 273:16305-16310. DOI 10.1074/jbc.273.26.16305 · PubMed
Other PDB entries of the same protein (UniProt P63103 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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