Gyf domain from human CD2BP2 protein. Determined by solution NMR. Released 5 Jan 2000.
Explore 1GYF in 3D Show helices and sheets RCSB PDB PDBe
1GYF contains 2 α-helices and 6 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 27 | 1 | 1 |
| β-strand | 28-31 | 4 | 2 |
| β-strand | 40-41 | 2 | 2 |
| β-strand | 45 | 1 | 1 |
| α-helix | 46-55 | 10 | |
| β-strand | 63-66 | 4 | 2 |
| β-strand | 75-76 | 2 | 2 |
| α-helix | 77-79 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (cytoplasmic domain binding protein (CD2BP2)) | A | protein | 62 | Homo sapiens | O95400 (AlphaFold model) |
>1GYF_1 PROTEIN (CYTOPLASMIC DOMAIN BINDING PROTEIN (CD2BP2)) (chains A) DVMWEYKWENTGDAELYGPFTSAQMQTWVSEGYFPDGVYCRKLDPPGGQFYNSKRIDFDL YT
The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. Freund, C., Dotsch, V., Nishizawa, K. et al. Nat Struct Biol (1999) 6:656-660. DOI 10.1038/10712 · PubMed
Other PDB entries of the same protein (UniProt O95400 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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