Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005179 | molecular_function | hormone activity |
| A | 0005576 | cellular_component | extracellular region |
| B | 0005179 | molecular_function | hormone activity |
| B | 0005576 | cellular_component | extracellular region |
| C | 0005179 | molecular_function | hormone activity |
| C | 0005576 | cellular_component | extracellular region |
| D | 0005179 | molecular_function | hormone activity |
| D | 0005576 | cellular_component | extracellular region |
| E | 0005179 | molecular_function | hormone activity |
| E | 0005576 | cellular_component | extracellular region |
| F | 0005179 | molecular_function | hormone activity |
| F | 0005576 | cellular_component | extracellular region |
| G | 0005179 | molecular_function | hormone activity |
| G | 0005576 | cellular_component | extracellular region |
| H | 0005179 | molecular_function | hormone activity |
| H | 0005576 | cellular_component | extracellular region |
| I | 0005179 | molecular_function | hormone activity |
| I | 0005576 | cellular_component | extracellular region |
| J | 0005179 | molecular_function | hormone activity |
| J | 0005576 | cellular_component | extracellular region |
| K | 0005179 | molecular_function | hormone activity |
| K | 0005576 | cellular_component | extracellular region |
| L | 0005179 | molecular_function | hormone activity |
| L | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue IPH A 101 |
| Chain | Residue |
| A | CYS6 |
| A | ILE10 |
| A | CYS11 |
| B | LEU11 |
| F | HIS5 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 101 |
| Chain | Residue |
| B | HIS10 |
| B | CL102 |
| F | HIS10 |
| J | HIS10 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 102 |
| Chain | Residue |
| B | HIS10 |
| B | ZN101 |
| F | HIS10 |
| J | HIS10 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue IPH C 101 |
| Chain | Residue |
| C | CYS6 |
| C | ILE10 |
| C | CYS11 |
| D | LEU11 |
| L | HIS5 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 101 |
| Chain | Residue |
| D | HIS10 |
| D | CL102 |
| H | HIS10 |
| L | HIS10 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 102 |
| Chain | Residue |
| D | HIS10 |
| D | ZN101 |
| H | HIS10 |
| L | HIS10 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue IPH E 101 |
| Chain | Residue |
| E | CYS6 |
| E | ILE10 |
| E | CYS11 |
| J | IPH101 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue IPH G 101 |
| Chain | Residue |
| G | CYS6 |
| G | ILE10 |
| G | CYS11 |
| H | LEU11 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue IPH H 102 |
| Chain | Residue |
| F | TYR16 |
| F | LEU17 |
| F | GLY20 |
| F | GLU21 |
| H | HIS5 |
| H | PRO28 |
| H | IPH101 |
| K | HOH208 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue IPH I 101 |
| Chain | Residue |
| I | CYS6 |
| I | ILE10 |
| I | CYS11 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue IPH J 102 |
| Chain | Residue |
| E | HOH209 |
| J | HIS5 |
| J | PRO28 |
| J | IPH101 |
| L | TYR16 |
| L | LEU17 |
| L | GLY20 |
| L | GLU21 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue IPH K 101 |
| Chain | Residue |
| K | CYS6 |
| K | ILE10 |
| K | CYS11 |
Functional Information from PROSITE/UniProt
| site_id | PS00262 |
| Number of Residues | 15 |
| Details | INSULIN Insulin family signature. CCTSiCSlyqLenyC |
| Chain | Residue | Details |
| A | CYS6-CYS20 | |
