An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth factor-BETA2. Determined by X-ray diffraction at 1.95 Å resolution. Released 31 Oct 1993.
Explore 1TFG in 3D Show helices and sheets RCSB PDB PDBe
1TFG contains 4 α-helices and 12 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 | 4-7 | 4 | |
| β-strand | 14 | 1 | 1 |
| β-strand | 16-18 | 3 | 2 |
| β-strand | 21-23 | 3 | 3 |
| α-helix | 24-28 | 5 | |
| β-strand | 33-35 | 3 | 4 |
| β-strand | 38-40 | 3 | 3 |
| β-strand | 43-45 | 3 | 2 |
| β-strand | 47 | 1 | 1 |
| β-strand | 54 | 1 | 5 |
| α-helix | 57-68 | 12 | |
| α-helix | 70-72 | 3 | |
| β-strand | 78-80 | 3 | 5 |
| β-strand | 83-92 | 10 | 4 |
| β-strand | 95-106 | 12 | 4 |
| β-strand | 109-111 | 3 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transforming growth factor, beta 2 | A | protein | 112 | Homo sapiens | P61812 (AlphaFold model) |
>1TFG_1 TRANSFORMING GROWTH FACTOR, BETA 2 (chains A) ALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSR VLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS
An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2. Schlunegger, M.P., Grutter, M.G. Nature (1992) 358:430-434. DOI 10.1038/358430a0 · PubMed
Other PDB entries of the same protein (UniProt P61812 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1TFG directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.