3NYL
The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain
Replaces: 1RW6Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016020 | cellular_component | membrane |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 191 |
Details | Domain: {"description":"E2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01218","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 63 |
Details | Region: {"description":"Heparin-binding"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 17 |
Details | Region: {"description":"Collagen-binding","evidences":[{"source":"PubMed","id":"8576160","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |