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 | ASP63 |
A | TYR95 |
A | THR120 |
A | ARG124 |
A | ALA126 |
A | GLY127 |
A | TYR188 |
A | HIS249 |
A | FE339 |
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 |
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
site_id | SWS_FT_FI1 |
Number of Residues | 322 |
Details | Domain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"P12346","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"O-linked (GalNAc...) serine","featureId":"CAR_000073"} |