Structural basis for the requirement of two phosphotyrosines in signaling mediated by Syk tyrosine kinase. Determined by solution NMR. Released 31 Jan 2006.
Explore 2FCI in 3D Show helices and sheets RCSB PDB PDBe
2FCI contains 2 α-helices and 8 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 | 19-27 | 9 | |
| β-strand | 34-38 | 5 | 1 |
| β-strand | 45-49 | 5 | 1 |
| β-strand | 50-51 | 2 | 2 |
| β-strand | 54-55 | 2 | 2 |
| β-strand | 59-60 | 2 | 1 |
| β-strand | 61 | 1 | 3 |
| β-strand | 67-68 | 2 | 3 |
| β-strand | 73-74 | 2 | 3 |
| α-helix | 78-86 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Doubly phosphorylated peptide derived from Syk kinase comprising residues 338-350 | B | protein | 14 | Q32PK0 (AlphaFold model) | |
| C-termainl SH2 domain from phospholipase C-gamma-1 comprising residues 663-759 | A | protein | 105 | Bos taurus | P08487 (AlphaFold model) |
>2FCI_1 Doubly phosphorylated peptide derived from Syk kinase comprising residues 338-350 (chains B) XDTEVYESPYADPE
>2FCI_2 C-termainl SH2 domain from phospholipase C-gamma-1 comprising residues 663-759 (chains A) GSPGIHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRV QQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEENSS
Structural basis for the requirement of two phosphotyrosine residues in signaling mediated by syk tyrosine kinase. Groesch, T.D., Zhou, F., Mattila, S. et al. J Mol Biol (2006) 356:1222-1236. DOI 10.1016/j.jmb.2005.11.095 · PubMed
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