Solution structures of human transforming growth factor alpha derived from 1*H NMR data. Determined by solution NMR. Released 15 Oct 1991.
Explore 4TGF in 3D Show helices and sheets RCSB PDB PDBe
4TGF contains 0 α-helices and 5 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 | 20-24 | 5 | 1 |
| β-strand | 29-33 | 5 | 1 |
| β-strand | 36 | 1 | 2 |
| β-strand | 38-39 | 2 | 2 |
| β-strand | 45-46 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Des-val-1,VAL-2,TRANSFORMING growth factor, alpha | A | protein | 50 | Homo sapiens | P01135 (AlphaFold model) |
>4TGF_1 DES-VAL-1,VAL-2,TRANSFORMING GROWTH FACTOR, ALPHA (chains A) VVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLA
Solution structures of human transforming growth factor alpha derived from 1H NMR data. Kline, T.P., Brown, F.K., Brown, S.C. et al. Biochemistry (1990) 29:7805-7813. DOI 10.1021/bi00486a005 · PubMed
Other PDB entries of the same protein (UniProt P01135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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