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 101 |
Chain | Residue |
A | CYS6 |
A | SER9 |
A | ILE10 |
A | CYS11 |
B | LEU11 |
F | HIS5 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ACN A 102 |
Chain | Residue |
I | LEU13 |
J | LEU17 |
A | LEU13 |
A | LEU16 |
B | VAL18 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 101 |
Chain | Residue |
B | HIS10 |
B | CL102 |
F | HIS10 |
L | HIS10 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CL B 102 |
Chain | Residue |
B | HIS10 |
B | ZN101 |
F | HIS10 |
L | HIS10 |
L | HOH221 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue ACN B 103 |
Chain | Residue |
B | ASN3 |
F | LEU6 |
L | HOH221 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue IPH C 101 |
Chain | Residue |
C | CYS6 |
C | ILE10 |
C | CYS11 |
D | LEU11 |
J | HIS5 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN D 101 |
Chain | Residue |
D | HIS10 |
H | HIS10 |
H | CL101 |
J | HIS10 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue IPH D 102 |
Chain | Residue |
D | LEU17 |
D | HOH202 |
D | HOH219 |
E | LEU13 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue IPH E 101 |
Chain | Residue |
E | CYS6 |
E | ILE10 |
E | CYS11 |
F | LEU11 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue IPH G 101 |
Chain | Residue |
G | CYS6 |
G | SER9 |
G | ILE10 |
G | CYS11 |
H | LEU11 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue CL H 101 |
Chain | Residue |
D | HIS10 |
D | ZN101 |
H | HIS10 |
J | HIS10 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue IPH I 101 |
Chain | Residue |
H | HIS5 |
I | CYS6 |
I | SER9 |
I | CYS11 |
J | LEU11 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue GOL J 101 |
Chain | Residue |
C | CYS7 |
D | ASN3 |
J | VAL2 |
J | ASN3 |
J | LEU6 |
J | HOH203 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue IPH K 101 |
Chain | Residue |
B | HIS5 |
K | CYS6 |
K | ILE10 |
K | CYS11 |
L | LEU11 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue GOL L 101 |
Chain | Residue |
B | VAL2 |
B | ASN3 |
B | LEU6 |
K | CYS7 |
L | ASN3 |
L | CYS7 |
Functional Information from PROSITE/UniProt
site_id | PS00262 |
Number of Residues | 15 |
Details | INSULIN Insulin family signature. CCTSiCSlyqLenyC |
Chain | Residue | Details |
A | CYS6-CYS20 | |