1KJS
NMR SOLUTION STRUCTURE OF C5A AT PH 5.2, 303K, 20 STRUCTURES
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS01177 |
Number of Residues | 35 |
Details | ANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCydGacvnnde.TCEqraarisl.GprCikafte.CC |
Chain | Residue | Details |
A | CYS21-CYS55 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 34 |
Details | Domain: {"description":"Anaphylatoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00022","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 29 |
Details | Region: {"description":"Involved in C5AR1 binding","evidences":[{"source":"PubMed","id":"9553099","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18536718","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CU7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KM9","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |