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 | 6 |
| Details | BINDING SITE FOR RESIDUE IPH A 22 |
| Chain | Residue |
| B | LEU11 |
| B | ALA14 |
| F | LEU6 |
| A | ILE10 |
| A | CYS11 |
| A | LEU16 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPH C 22 |
| Chain | Residue |
| C | ILE10 |
| C | CYS11 |
| C | LEU16 |
| D | LEU11 |
| D | ALA14 |
| L | LEU6 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPH E 22 |
| Chain | Residue |
| E | ILE10 |
| E | CYS11 |
| E | LEU16 |
| F | LEU11 |
| F | ALA14 |
| J | LEU6 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPH G 22 |
| Chain | Residue |
| D | LEU6 |
| G | ILE10 |
| G | CYS11 |
| G | LEU16 |
| H | LEU11 |
| H | ALA14 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPH I 22 |
| Chain | Residue |
| B | LEU6 |
| I | ILE10 |
| I | CYS11 |
| I | LEU16 |
| J | LEU11 |
| J | ALA14 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPH K 22 |
| Chain | Residue |
| H | LEU6 |
| K | ILE10 |
| K | CYS11 |
| K | LEU16 |
| L | LEU11 |
| L | ALA14 |
| site_id | ZN1 |
| Number of Residues | 3 |
| Details | IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. |
| Chain | Residue |
| B | HIS10 |
| F | HIS10 |
| J | HIS10 |
| site_id | ZN2 |
| Number of Residues | 3 |
| Details | IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. |
| Chain | Residue |
| D | HIS10 |
| H | HIS10 |
| L | HIS10 |
Functional Information from PROSITE/UniProt
| site_id | PS00262 |
| Number of Residues | 15 |
| Details | INSULIN Insulin family signature. CCTSiCSlyqLenyC |
| Chain | Residue | Details |
| A | CYS6-CYS20 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 120 |
| Details | Peptide: {"description":"Insulin A chain","featureId":"PRO_0000015821"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 174 |
| Details | Peptide: {"description":"Insulin B chain","featureId":"PRO_0000015819"} |
