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2I9B

Crystal structure of ATF-urokinase receptor complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0008236molecular_functionserine-type peptidase activity
A0031639biological_processplasminogen activation
B0008236molecular_functionserine-type peptidase activity
B0031639biological_processplasminogen activation
C0008236molecular_functionserine-type peptidase activity
C0031639biological_processplasminogen activation
D0008236molecular_functionserine-type peptidase activity
D0031639biological_processplasminogen activation
E0030162biological_processregulation of proteolysis
E0030377molecular_functionurokinase plasminogen activator receptor activity
E0038195biological_processurokinase plasminogen activator signaling pathway
F0030162biological_processregulation of proteolysis
F0030377molecular_functionurokinase plasminogen activator receptor activity
F0038195biological_processurokinase plasminogen activator signaling pathway
G0030162biological_processregulation of proteolysis
G0030377molecular_functionurokinase plasminogen activator receptor activity
G0038195biological_processurokinase plasminogen activator signaling pathway
H0030162biological_processregulation of proteolysis
H0030377molecular_functionurokinase plasminogen activator receptor activity
H0038195biological_processurokinase plasminogen activator signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues13
DetailsKRINGLE_1 Kringle domain signature. YCRNpdnrrrp.WC
ChainResidueDetails
ATYR101-CYS113

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CnCpkKfgGQhC
ChainResidueDetails
ACYS31-CYS42

site_idPS00983
Number of Residues44
DetailsLY6_UPAR Ly-6 / u-PAR domain signature. RCMqCktngd...Crve.....ECAlgqdlCrttivrlweegeelelveks....C
ChainResidueDetails
EARG2-CYS45
EGLU94-CYS147
EGLN193-CYS247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues324
DetailsDomain: {"description":"Kringle","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues92
DetailsRegion: {"description":"Binds urokinase plasminogen activator surface receptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (Fuc) threonine","evidences":[{"source":"PubMed","id":"2023947","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues182
DetailsDomain: {"description":"UPAR/Ly6 1"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Cleavage; by U-PA"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15861141","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15861141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16456079","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22285761","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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