Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005179 | molecular_function | hormone activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0006144 | biological_process | purine nucleobase metabolic process |
A | 0007165 | biological_process | signal transduction |
A | 0035578 | cellular_component | azurophil granule lumen |
A | 0042802 | molecular_function | identical protein binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070324 | molecular_function | thyroid hormone binding |
B | 0005179 | molecular_function | hormone activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0006144 | biological_process | purine nucleobase metabolic process |
B | 0007165 | biological_process | signal transduction |
B | 0035578 | cellular_component | azurophil granule lumen |
B | 0042802 | molecular_function | identical protein binding |
B | 0070062 | cellular_component | extracellular exosome |
B | 0070324 | molecular_function | thyroid hormone binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 201 |
Chain | Residue |
A | PHE44 |
A | GLU66 |
A | ASP99 |
A | EDO202 |
A | HOH369 |
A | HOH410 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 202 |
Chain | Residue |
A | HOH410 |
A | GLU66 |
A | ASP99 |
A | EDO201 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 203 |
Chain | Residue |
A | SER23 |
A | PRO24 |
A | VAL122 |
A | THR123 |
A | EDO204 |
A | HOH384 |
A | HOH408 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 204 |
Chain | Residue |
A | PRO24 |
A | ILE26 |
A | GLU51 |
A | EDO203 |
A | HOH357 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAR A 205 |
Chain | Residue |
A | LYS15 |
A | LYS15 |
A | LEU17 |
A | LEU17 |
A | ALA108 |
A | ALA108 |
A | LEU110 |
A | SER117 |
A | THR119 |
A | THR119 |
A | HOH338 |
A | HOH338 |
A | HOH397 |
A | HOH404 |
A | HOH404 |
A | HOH411 |
A | HOH411 |
B | SER115 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 206 |
Chain | Residue |
A | ARG34 |
A | SER46 |
A | GLY47 |
A | HIS56 |
A | GLU66 |
A | HOH311 |
A | HOH383 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 207 |
Chain | Residue |
A | ASP74 |
A | LYS76 |
A | SER77 |
A | GLU89 |
A | HOH308 |
A | HOH319 |
A | HOH327 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 208 |
Chain | Residue |
A | ALA37 |
A | LYS48 |
A | GLU54 |
A | LEU55 |
A | HIS56 |
A | HOH391 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 201 |
Chain | Residue |
B | PHE44 |
B | ALA45 |
B | GLY57 |
B | LEU58 |
B | GLU63 |
B | GLU66 |
B | ASP99 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NAR B 202 |
Chain | Residue |
B | LYS15 |
B | LYS15 |
B | LEU17 |
B | ALA108 |
B | ALA108 |
B | LEU110 |
B | SER117 |
B | THR119 |
B | THR119 |
B | VAL121 |
B | HOH393 |
B | HOH397 |
B | HOH407 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA B 203 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 204 |
Chain | Residue |
B | ARG34 |
B | LYS35 |
B | GLY67 |
B | ILE68 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 205 |
Chain | Residue |
A | HIS90 |
A | GLU92 |
A | HOH375 |
B | TRP41 |
B | LYS70 |
B | GLU92 |
B | HOH338 |
B | HOH375 |
Functional Information from PROSITE/UniProt
site_id | PS00768 |
Number of Residues | 16 |
Details | TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV |
Chain | Residue | Details |
A | LYS15-VAL30 | |
site_id | PS00769 |
Number of Residues | 13 |
Details | TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS |
Chain | Residue | Details |
A | TYR105-SER117 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS15 | |
A | GLU54 | |
A | SER117 | |
B | LYS15 | |
B | GLU54 | |
B | SER117 | |
Chain | Residue | Details |
A | CYS10 | |
B | CYS10 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012 |
Chain | Residue | Details |
A | GLU42 | |
B | GLU42 | |
Chain | Residue | Details |
A | SER52 | |
B | SER52 | |
Chain | Residue | Details |
A | ASN98 | |
B | ASN98 | |