Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CO3 A 338 |
Chain | Residue |
A | ALA126 |
A | GLY127 |
A | TYR188 |
A | HIS249 |
A | FE339 |
A | ASP63 |
A | TYR95 |
A | THR120 |
A | ARG124 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 339 |
Chain | Residue |
A | ASP63 |
A | TYR95 |
A | TYR188 |
A | HIS249 |
A | CO3338 |
site_id | FE |
Number of Residues | 5 |
Details | FERRIC ION BINDING SITE. CARBONATE AND ARGININE 124 BOTH DISORDERED WITH TWO DISTINCT CONFORMATIONS. |
Chain | Residue |
A | ASP63 |
A | TYR95 |
A | TYR188 |
A | HIS249 |
A | CO3338 |
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 |
A | TYR95-ASP104 | |
site_id | PS00206 |
Number of Residues | 17 |
Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF |
Chain | Residue | Details |
A | TYR188-PHE204 | |
site_id | PS00207 |
Number of Residues | 31 |
Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV |
Chain | Residue | Details |
A | GLN222-VAL252 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP63 | |
A | TYR95 | |
A | TYR188 | |
A | HIS249 | |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | THR120 | |
A | ARG124 | |
A | ALA126 | |
A | GLY127 | |
Chain | Residue | Details |
A | ARG23 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (GalNAc...) serine |
Chain | Residue | Details |
A | SER32 | |