1SUV
Structure of Human Transferrin Receptor-Transferrin Complex
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. YyAVAVVKKD |
| Chain | Residue | Details |
| C | TYR95-ASP104 | |
| E | TYR425-SER434 |
| site_id | PS00206 |
| Number of Residues | 17 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF |
| Chain | Residue | Details |
| C | TYR188-PHE204 | |
| E | TYR514-PHE529 |
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV |
| Chain | Residue | Details |
| C | GLN222-VAL252 | |
| E | ASP555-VAL585 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 180 |
| Details | Domain: {"description":"PA"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 382 |
| Details | Region: {"description":"Ligand-binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Cell attachment site; required for binding to transferrin"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10531064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CX8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10531064","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CX8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000173","evidences":[{"source":"PubMed","id":"10531064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7780197","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CX8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 644 |
| Details | Domain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"P12346","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) serine","featureId":"CAR_000073"} |
| Chain | Residue | Details |
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 |






