2FD6
Structure of Human Urokinase Plasminogen Activator in Complex with Urokinase Receptor and an anti-upar antibody at 1.9 A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| H | 0002250 | biological_process | adaptive immune response |
| H | 0002376 | biological_process | immune system process |
| H | 0005576 | cellular_component | extracellular region |
| H | 0019814 | cellular_component | immunoglobulin complex |
| L | 0002250 | biological_process | adaptive immune response |
| L | 0002376 | biological_process | immune system process |
| L | 0019814 | cellular_component | immunoglobulin complex |
| L | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00021 |
| Number of Residues | 13 |
| Details | KRINGLE_1 Kringle domain signature. YCRNpdnrrrp.WC |
| Chain | Residue | Details |
| A | TYR101-CYS113 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CnCpkKfgGQhC |
| Chain | Residue | Details |
| A | CYS31-CYS42 |
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
| Chain | Residue | Details |
| L | TYR191-HIS197 |
| site_id | PS00983 |
| Number of Residues | 44 |
| Details | LY6_UPAR Ly-6 / u-PAR domain signature. RCMqCktngd...Crve.....ECAlgqdlCrttivrlweegeelelveks....C |
| Chain | Residue | Details |
| U | ARG2-CYS45 | |
| U | GLU94-CYS147 | |
| U | GLN193-CYS247 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 81 |
| Details | Domain: {"description":"Kringle","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 23 |
| Details | Region: {"description":"Binds urokinase plasminogen activator surface receptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Fuc) threonine","evidences":[{"source":"PubMed","id":"2023947","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15861141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16456079","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22285761","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15861141","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15861141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16456079","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22285761","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
