Crystal structure of Latency Associated Peptide unbound to TGF-beta1. Determined by X-ray diffraction at 3.5 Å resolution. Released 11 Mar 2020.
Explore 6P7J in 3D Show helices and sheets RCSB PDB PDBe
6P7J contains 2 α-helices and 11 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 | 79-84 | 6 | 1 |
| β-strand | 103-106 | 4 | 2 |
| α-helix | 108-110 | 3 | |
| β-strand | 120-129 | 10 | 1 |
| β-strand | 136-143 | 8 | 2 |
| β-strand | 149-157 | 9 | 2 |
| β-strand | 164-169 | 6 | 1 |
| α-helix | 171-179 | 9 | |
| β-strand | 185-191 | 7 | 2 |
| β-strand | 193-198 | 6 | 3 |
| β-strand | 201-206 | 6 | 3 |
| β-strand | 218 | 1 | 1 |
| β-strand | 227-232 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transforming growth factor beta-1 proprotein | A | protein | 255 | Homo sapiens | P01137 (AlphaFold model) |
>6P7J_1 Transforming growth factor beta-1 proprotein (chains A) LSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVA GESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVL LSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLS RGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQ HLQSSRHRAHHHHHH
Structural insights into conformational switching in latency-associated peptide between transforming growth factor beta-1 bound and unbound states. Stachowski, T.R., Snell, M.E., Snell, E.H. IUCrJ (2020) 7:238-252. DOI 10.1107/S205225251901707X
Other PDB entries of the same protein (UniProt P01137 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6P7J 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.