Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
Functional Information from PROSITE/UniProt
site_id | PS00205 |
Number of Residues | 10 |
Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG |
Chain | Residue | Details |
A | TYR92-GLY101 | |
site_id | PS00206 |
Number of Residues | 17 |
Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFHCLkdgkGDVAF |
Chain | Residue | Details |
A | TYR191-PHE207 | |
site_id | PS00207 |
Number of Residues | 31 |
Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLClDgsrqp...VdnyktCnwArvaaHaVV |
Chain | Residue | Details |
A | GLU223-VAL253 | |
site_id | PS00962 |
Number of Residues | 12 |
Details | RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. VpSLMDSQLYLG |
Chain | Residue | Details |
A | VAL310-GLY321 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP60 | |
A | TYR92 | |
A | THR117 | |
A | ARG121 | |
A | ALA123 | |
A | GLY124 | |
A | TYR191 | |
A | HIS250 | |