Functional Information from GO Data
Chain | GOid | namespace | contents |
X | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE X 500 |
Chain | Residue |
X | ASP63 |
X | TYR95 |
X | TYR188 |
X | HIS249 |
X | CO3600 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CO3 X 600 |
Chain | Residue |
X | SER125 |
X | ALA126 |
X | GLY127 |
X | TYR188 |
X | FE500 |
X | ASP63 |
X | TYR95 |
X | THR120 |
X | ARG124 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K X 601 |
Chain | Residue |
X | ALA151 |
X | ASN152 |
X | PHE154 |
X | GLN169 |
Functional Information from PROSITE/UniProt
site_id | PS00205 |
Number of Residues | 10 |
Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD |
Chain | Residue | Details |
X | TYR95-ASP104 | |
site_id | PS00206 |
Number of Residues | 17 |
Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF |
Chain | Residue | Details |
X | TYR188-PHE204 | |
site_id | PS00207 |
Number of Residues | 31 |
Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV |
Chain | Residue | Details |
X | GLN222-VAL252 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
X | ASP63 | |
X | TYR95 | |
X | TYR188 | |
X | HIS249 | |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
X | THR120 | |
X | ARG124 | |
X | ALA126 | |
X | GLY127 | |
Chain | Residue | Details |
X | ARG23 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (GalNAc...) serine |
Chain | Residue | Details |
X | SER32 | |