5AO6
Endo180 D1-4, trigonal form
Functional Information from PROSITE/UniProt
site_id | PS00023 |
Number of Residues | 42 |
Details | FN2_1 Fibronectin type-II collagen-binding domain signature. CtiPFkYdnqwfhgCtstgredghlWCattqDYgkderWgFC |
Chain | Residue | Details |
A | CYS187-CYS228 |
site_id | PS00615 |
Number of Residues | 25 |
Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CGvirtessgg...WQNRDCsialp.YVC |
Chain | Residue | Details |
A | CYS335-CYS359 | |
A | CYS481-CYS504 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 96 |
Details | Domain: {"description":"Fibronectin type-II","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 232 |
Details | Domain: {"description":"C-type lectin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 232 |
Details | Domain: {"description":"C-type lectin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |