Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006144 | biological_process | purine nucleobase metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019628 | biological_process | urate catabolic process |
A | 0033971 | molecular_function | hydroxyisourate hydrolase activity |
A | 0042802 | molecular_function | identical protein binding |
B | 0006144 | biological_process | purine nucleobase metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019628 | biological_process | urate catabolic process |
B | 0033971 | molecular_function | hydroxyisourate hydrolase activity |
B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 200 |
Chain | Residue |
A | HIS14 |
A | HIS14 |
A | ARG49 |
A | TYR118 |
A | TYR118 |
A | SER121 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 201 |
Chain | Residue |
B | ARG49 |
B | HIS105 |
B | SER121 |
Functional Information from PROSITE/UniProt
site_id | PS00768 |
Number of Residues | 16 |
Details | TRANSTHYRETIN_1 Transthyretin signature 1. HILDltcGkPAanVkI |
Chain | Residue | Details |
A | HIS14-ILE29 | |
site_id | PS00769 |
Number of Residues | 13 |
Details | TRANSTHYRETIN_2 Transthyretin signature 2. YHIPllLSPFGYQ |
Chain | Residue | Details |
A | TYR104-GLN116 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS14 | |
A | ARG49 | |
A | TYR118 | |
B | HIS14 | |
B | ARG49 | |
B | TYR118 | |