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 1022 |
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 1030 |
Chain | Residue |
B | HIS10 |
B | CL1031 |
F | HIS10 |
J | HIS10 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 1031 |
Chain | Residue |
B | HIS10 |
B | ZN1030 |
F | HIS10 |
J | HIS10 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPH C 1022 |
Chain | Residue |
C | CYS6 |
C | SER9 |
C | ILE10 |
C | CYS11 |
D | LEU11 |
L | HIS5 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 1029 |
Chain | Residue |
D | HIS10 |
D | CL1030 |
H | HIS10 |
L | HIS10 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL D 1030 |
Chain | Residue |
D | HIS10 |
D | ZN1029 |
H | HIS10 |
L | HIS10 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPH E 1022 |
Chain | Residue |
E | CYS6 |
E | ILE10 |
E | CYS11 |
F | LEU11 |
J | HIS5 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IPH H 1029 |
Chain | Residue |
G | CYS6 |
G | ILE10 |
G | CYS11 |
H | LEU11 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPH I 1022 |
Chain | Residue |
B | HIS5 |
I | CYS6 |
I | ILE10 |
I | CYS11 |
J | LEU11 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPH K 1022 |
Functional Information from PROSITE/UniProt
site_id | PS00262 |
Number of Residues | 15 |
Details | INSULIN Insulin family signature. CCTSiCSlyqLenyC |
Chain | Residue | Details |
A | CYS6-CYS20 | |