Insulin glulisine. Determined by X-ray diffraction at 1.26 Å resolution. Released 3 Jul 2019.
Explore 6GV0 in 3D Show helices and sheets RCSB PDB PDBe
6GV0 contains 11 α-helices and 8 β-strands across 4 chains. 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 | 4 | 1 | 1 |
| α-helix | 8-19 | 12 | |
| α-helix | 20-22 | 3 | |
| β-strand | 24-26 | 3 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 3 |
| α-helix | 9-19 | 11 | |
| α-helix | 20-22 | 3 | |
| β-strand | 24-26 | 3 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-3 | 2 | |
| α-helix | 4-8 | 5 | |
| β-strand | 11 | 1 | 1 |
| α-helix | 13-16 | 4 | |
| α-helix | 17-19 | 3 | |
| β-strand | 20 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-8 | 7 | |
| β-strand | 11 | 1 | 3 |
| α-helix | 13-16 | 4 | |
| α-helix | 17-19 | 3 | |
| β-strand | 20 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Insulin | G, I | protein | 21 | Homo sapiens | P01308 (AlphaFold model) |
| Insulin | B, D | protein | 30 | Homo sapiens | P01308 (AlphaFold model) |
>6GV0_1 Insulin (chains G, I) GIVEQCCTSICSLYQLENYCN
>6GV0_2 Insulin (chains B, D) FVKQHLCGSHLVEALYLVCGERGFFYTPET
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Water and common crystallization additives (FMT) are not listed.
Analysis of insulin glulisine at the molecular level by X-ray crystallography and biophysical techniques. Gillis, R.B., Solomon, H.V., Govada, L. et al. Sci Rep (2021) 11:1737-1737. DOI 10.1038/s41598-021-81251-2 · PubMed
Other PDB entries of the same protein (UniProt P01308 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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