1CX8
CRYSTAL STRUCTURE OF THE ECTODOMAIN OF HUMAN TRANSFERRIN RECEPTOR
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 | 0004998 | molecular_function | transferrin receptor activity |
C | 0033572 | biological_process | transferrin transport |
D | 0004998 | molecular_function | transferrin receptor activity |
D | 0033572 | biological_process | transferrin transport |
E | 0004998 | molecular_function | transferrin receptor activity |
E | 0033572 | biological_process | transferrin transport |
F | 0004998 | molecular_function | transferrin receptor activity |
F | 0033572 | biological_process | transferrin transport |
G | 0004998 | molecular_function | transferrin receptor activity |
G | 0033572 | biological_process | transferrin transport |
H | 0004998 | molecular_function | transferrin receptor activity |
H | 0033572 | biological_process | transferrin transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10531064, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973, ECO:0007744|PDB:1CX8 |
Chain | Residue | Details |
A | ASN251 | |
B | ASN251 | |
C | ASN251 | |
D | ASN251 | |
E | ASN251 | |
F | ASN251 | |
G | ASN251 | |
H | ASN251 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10531064, ECO:0007744|PDB:1CX8 |
Chain | Residue | Details |
A | ASN317 | |
B | ASN317 | |
C | ASN317 | |
D | ASN317 | |
E | ASN317 | |
F | ASN317 | |
G | ASN317 | |
H | ASN317 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10531064, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7780197, ECO:0007744|PDB:1CX8 |
Chain | Residue | Details |
A | ASN727 | |
B | ASN727 | |
C | ASN727 | |
D | ASN727 | |
E | ASN727 | |
F | ASN727 | |
G | ASN727 | |
H | ASN727 |
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 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1amp |
Chain | Residue | Details |
C | GLY456 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1amp |
Chain | Residue | Details |
D | GLY456 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1amp |
Chain | Residue | Details |
E | GLY456 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1amp |
Chain | Residue | Details |
F | GLY456 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1amp |
Chain | Residue | Details |
G | GLY456 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1amp |
Chain | Residue | Details |
H | GLY456 |