NMR structure of the Y174 autoinhibited dbl homology domain. Determined by solution NMR. Released 15 Sept 2000.
Explore 1F5X in 3D Show helices and sheets RCSB PDB PDBe
1F5X contains 13 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 3-10 | 8 | |
| α-helix | 24-26 | 3 | |
| α-helix | 27-46 | 20 | |
| α-helix | 54-57 | 4 | |
| α-helix | 63-69 | 7 | |
| α-helix | 73-92 | 20 | |
| α-helix | 96-98 | 3 | |
| α-helix | 99-104 | 6 | |
| α-helix | 107-110 | 4 | |
| α-helix | 112-133 | 22 | |
| α-helix | 135-145 | 11 | |
| α-helix | 162-177 | 16 | |
| α-helix | 185-203 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho-gef vav | A | protein | 208 | Mus musculus | P27870 (AlphaFold model) |
>1F5X_1 RHO-GEF VAV (chains A) MKGDEIYEDLMRLESVPTPPKMTEYDKRCCCLREIQQTEEKYTDTLGSIQQHFMKPLQRF LKPQDMETIFVNIEELFSVHTHFLKELKDALAGPGATTLYQVFIKYKERFLVYGRYCSQV ESASKHLDQVATAREDVQMKLEECSQRANNGRFTLRDLLMVPMQRVLKYHLLLQELVKHT QDATEKENLRLALDAMRDLAQCVNEVKR
Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation. Aghazadeh, B., Lowry, W.E., Huang, X.Y. et al. Cell (2000) 102:625-633. DOI 10.1016/S0092-8674(00)00085-4 · PubMed
Other PDB entries of the same protein (UniProt P27870 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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