Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005179 | molecular_function | hormone activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0008083 | molecular_function | growth factor activity |
Functional Information from PDB Data
| site_id | AR |
| Number of Residues | 3 |
| Details | THESE THREE AROMATIC RESIDUES ARE INVOLVED IN BINDING TO THE IGF RECEPTORS. THEY ARE CLOSE IN SPACE TO THE HYDROPHOBIC CORE FORMED BY THE THREE HELICES. PHE 36 AND PHE 38 POINT INTO THE HYDROPHOBIC CORE, WHILE THE AROMATIC RING OF TYR 37 POINTS AWAY FROM THE HYDROPHOBIC CORE. THE RESPECTIVE RESIDUES IN IGF-I ARE PHE 23, TYR 24 AND PHE |
| Chain | Residue |
| A | PHE36 |
| A | TYR37 |
| A | PHE38 |
| site_id | NTR |
| Number of Residues | 3 |
| Details | THE N TERMINUS OF IGF-I IS IMPORTANT FOR BINDING TO IGF BINDING PROTEINS. RESIDUES 1-3 OF IGF-I ARE IMPLICATED AS HAVING A ROLE ALTHOUGH GLU 3 IS MOST IMPORTANT. IN LONG-[ARG3]-IGF-I THE RESPECTIVE RESIDUES ARE GLY 14, PRO 15 AND ARG 16. |
| Chain | Residue |
| A | ARG16 |
| A | PRO15 |
| A | GLY14 |
Functional Information from PROSITE/UniProt
| site_id | PS00262 |
| Number of Residues | 15 |
| Details | INSULIN Insulin family signature. CCFRsCDlrrLemyC |
| Chain | Residue | Details |
| A | CYS60-CYS74 | |
