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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 301 |
Chain | Residue |
B | HIS10 |
F | HIS10 |
J | HIS10 |
J | CL303 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 302 |
Chain | Residue |
D | HIS10 |
D | CL304 |
H | HIS10 |
L | HIS10 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL J 303 |
Chain | Residue |
B | ZN301 |
F | HIS10 |
J | HIS10 |
B | HIS10 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL D 304 |
Chain | Residue |
D | HIS10 |
D | ZN302 |
H | HIS10 |
L | HIS10 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA J 305 |
Chain | Residue |
E | HOH96 |
J | PHE1 |
J | ASN3 |
J | HOH309 |
J | HOH313 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE RCO A 306 |
Chain | Residue |
A | CYS6 |
A | SER9 |
A | ILE10 |
A | CYS11 |
A | HOH25 |
B | LEU11 |
B | ALA14 |
F | HIS5 |
H | LEU17 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE RCO C 307 |
Chain | Residue |
C | CYS6 |
C | SER9 |
C | ILE10 |
C | CYS11 |
C | HOH308 |
D | LEU11 |
D | ALA14 |
J | LEU17 |
L | HIS5 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE RCO E 308 |
Chain | Residue |
E | CYS6 |
E | SER9 |
E | ILE10 |
E | CYS11 |
E | HOH32 |
F | ALA14 |
J | HIS5 |
L | LEU17 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE RCO G 309 |
Chain | Residue |
B | LEU17 |
D | HIS5 |
G | CYS6 |
G | SER9 |
G | ILE10 |
G | CYS11 |
G | HOH310 |
H | LEU11 |
H | ALA14 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE RCO I 310 |
Chain | Residue |
B | HIS5 |
D | LEU17 |
I | CYS6 |
I | ILE10 |
I | CYS11 |
I | HOH311 |
J | LEU11 |
J | ALA14 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE RCO K 311 |
Chain | Residue |
F | LEU17 |
H | HIS5 |
K | CYS6 |
K | SER9 |
K | ILE10 |
K | CYS11 |
K | HOH312 |
L | LEU11 |
L | ALA14 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE RCO A 312 |
Chain | Residue |
A | LEU13 |
A | GLU17 |
G | LEU13 |
G | TYR14 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE RCO B 313 |
Chain | Residue |
B | ASN3 |
B | LEU6 |
F | ASN3 |
F | HOH45 |
I | HOH316 |
J | ASN3 |
Functional Information from PROSITE/UniProt
site_id | PS00262 |
Number of Residues | 15 |
Details | INSULIN Insulin family signature. CCTSiCSlyqLenyC |
Chain | Residue | Details |
A | CYS6-CYS20 | |