The solution structure of a well-folded peptide based on the 31-residue amino-terminal subdomain of human granulin a. Determined by solution NMR. Released 1 Nov 2000.
Explore 1G26 in 3D Show helices and sheets RCSB PDB PDBe
1G26 contains 0 α-helices and 4 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 | 2-5 | 4 | 1 |
| β-strand | 8-10 | 3 | 1 |
| β-strand | 14-18 | 5 | 2 |
| β-strand | 24-28 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Granulin a | A | protein | 31 | P28799 (AlphaFold model) |
>1G26_1 GRANULIN A (chains A) VVHCDMEVICPDGYTCCRLPSGAWGCCPFTQ
Design and solution structure of a well-folded stack of two beta-hairpins based on the amino-terminal fragment of human granulin A. Tolkatchev, D., Ng, A., Vranken, W. et al. Biochemistry (2000) 39:2878-2886. DOI 10.1021/bi992130u · PubMed
Other PDB entries of the same protein (UniProt P28799 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1G26 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.