Solution structure of human insulin-like growth factor II relationship to receptor and binding protein interactions. Determined by solution NMR. Released 14 Feb 1995.
Explore 1IGL in 3D Show helices and sheets RCSB PDB PDBe
1IGL contains 3 α-helices and 2 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 | 14-20 | 7 | |
| β-strand | 26 | 1 | 1 |
| α-helix | 44-48 | 5 | |
| α-helix | 54-59 | 6 | |
| β-strand | 60 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Insulin-like growth factor II | A | protein | 67 | Homo sapiens | P01344 (AlphaFold model) |
>1IGL_1 INSULIN-LIKE GROWTH FACTOR II (chains A) AYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYC ATPAKSE
Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions. Torres, A.M., Forbes, B.E., Aplin, S.E. et al. J Mol Biol (1995) 248:385-401. PubMed
Other PDB entries of the same protein (UniProt P01344 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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