2I9B
Crystal structure of ATF-urokinase receptor complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0031639 | biological_process | plasminogen activation |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0031639 | biological_process | plasminogen activation |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0031639 | biological_process | plasminogen activation |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0031639 | biological_process | plasminogen activation |
| E | 0030162 | biological_process | regulation of proteolysis |
| E | 0030377 | molecular_function | urokinase plasminogen activator receptor activity |
| E | 0038195 | biological_process | urokinase plasminogen activator signaling pathway |
| F | 0030162 | biological_process | regulation of proteolysis |
| F | 0030377 | molecular_function | urokinase plasminogen activator receptor activity |
| F | 0038195 | biological_process | urokinase plasminogen activator signaling pathway |
| G | 0030162 | biological_process | regulation of proteolysis |
| G | 0030377 | molecular_function | urokinase plasminogen activator receptor activity |
| G | 0038195 | biological_process | urokinase plasminogen activator signaling pathway |
| H | 0030162 | biological_process | regulation of proteolysis |
| H | 0030377 | molecular_function | urokinase plasminogen activator receptor activity |
| H | 0038195 | biological_process | urokinase plasminogen activator signaling pathway |
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 | PS00983 |
| Number of Residues | 44 |
| Details | LY6_UPAR Ly-6 / u-PAR domain signature. RCMqCktngd...Crve.....ECAlgqdlCrttivrlweegeelelveks....C |
| Chain | Residue | Details |
| E | ARG2-CYS45 | |
| E | GLU94-CYS147 | |
| E | GLN193-CYS247 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | SITE: Cleavage; by U-PA |
| Chain | Residue | Details |
| E | ARG83 | |
| E | ARG89 | |
| F | ARG83 | |
| F | ARG89 | |
| G | ARG83 | |
| G | ARG89 | |
| H | ARG83 | |
| H | ARG89 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15861141, ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761 |
| Chain | Residue | Details |
| E | ASN52 | |
| F | ASN52 | |
| G | ASN52 | |
| H | ASN52 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15861141 |
| Chain | Residue | Details |
| E | GLN162 | |
| E | GLN233 | |
| F | GLN162 | |
| F | GLN233 | |
| G | GLN162 | |
| G | GLN233 | |
| H | GLN162 | |
| H | GLN233 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15861141, ECO:0000269|PubMed:16456079 |
| Chain | Residue | Details |
| E | GLN172 | |
| F | GLN172 | |
| G | GLN172 | |
| H | GLN172 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22285761 |
| Chain | Residue | Details |
| E | GLN200 | |
| F | GLN200 | |
| G | GLN200 | |
| H | GLN200 |
