Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004998 | molecular_function | transferrin receptor activity |
| A | 0033572 | biological_process | transferrin transport |
| B | 0004998 | molecular_function | transferrin receptor activity |
| B | 0033572 | biological_process | transferrin transport |
| C | 0005576 | cellular_component | extracellular region |
| D | 0005576 | cellular_component | extracellular region |
| E | 0005576 | cellular_component | extracellular region |
| F | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO3 C 338 |
| Chain | Residue |
| C | ASP63 |
| C | TYR95 |
| C | THR120 |
| C | ARG124 |
| C | ALA126 |
| C | GLY127 |
| C | TYR188 |
| C | HIS249 |
| C | FE339 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE C 339 |
| Chain | Residue |
| C | ASP63 |
| C | TYR95 |
| C | TYR188 |
| C | HIS249 |
| C | CO3338 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO3 D 338 |
| Chain | Residue |
| D | ASP63 |
| D | TYR95 |
| D | THR120 |
| D | ARG124 |
| D | ALA126 |
| D | GLY127 |
| D | TYR188 |
| D | HIS249 |
| D | FE339 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE D 339 |
| Chain | Residue |
| D | ASP63 |
| D | TYR95 |
| D | TYR188 |
| D | HIS249 |
| D | CO3338 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CO3 E 701 |
| Chain | Residue |
| E | ASP392 |
| E | TYR425 |
| E | THR451 |
| E | ARG455 |
| E | THR456 |
| E | ALA457 |
| E | GLY458 |
| E | TYR514 |
| E | HIS582 |
| E | FE703 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE E 703 |
| Chain | Residue |
| E | ASP392 |
| E | TYR425 |
| E | TYR514 |
| E | HIS582 |
| E | CO3701 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CO3 F 701 |
| Chain | Residue |
| F | ASP392 |
| F | TYR425 |
| F | THR451 |
| F | ARG455 |
| F | THR456 |
| F | ALA457 |
| F | GLY458 |
| F | TYR514 |
| F | HIS582 |
| F | FE703 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE F 703 |
| Chain | Residue |
| F | ASP392 |
| F | TYR425 |
| F | TYR514 |
| F | HIS582 |
| F | CO3701 |
Functional Information from PROSITE/UniProt
| site_id | PS00205 |
| Number of Residues | 10 |
| Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YlSVAVVKKS |
| Chain | Residue | Details |
| E | TYR425-SER434 | |
| C | TYR95-ASP104 | |
| site_id | PS00206 |
| Number of Residues | 16 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YtGAFRCLvek.GDVAF |
| Chain | Residue | Details |
| E | TYR514-PHE529 | |
| C | TYR188-PHE204 | |
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. DFeLLClDgtrkp...VseahnChlAkapnHaVV |
| Chain | Residue | Details |
| E | ASP555-VAL585 | |
| C | GLN222-VAL252 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| C | ASP63 | |
| C | TYR95 | |
| C | TYR188 | |
| C | HIS249 | |
| D | ASP63 | |
| D | TYR95 | |
| D | TYR188 | |
| D | HIS249 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| C | THR120 | |
| C | ARG124 | |
| C | ALA126 | |
| C | GLY127 | |
| D | THR120 | |
| D | ARG124 | |
| D | ALA126 | |
| D | GLY127 | |
| Chain | Residue | Details |
| C | ARG23 | |
| D | ARG23 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GalNAc...) serine |
| Chain | Residue | Details |
| C | SER32 | |
| D | SER32 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| A | GLY456 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| B | GLY456 | |
