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3BT2

Structure of urokinase receptor, urokinase and vitronectin complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0005044molecular_functionscavenger receptor activity
B0006955biological_processimmune response
B0030247molecular_functionpolysaccharide binding
U0001934biological_processpositive regulation of protein phosphorylation
U0005102molecular_functionsignaling receptor binding
U0005515molecular_functionprotein binding
U0005576cellular_componentextracellular region
U0005788cellular_componentendoplasmic reticulum lumen
U0005789cellular_componentendoplasmic reticulum membrane
U0005886cellular_componentplasma membrane
U0005925cellular_componentfocal adhesion
U0006935biological_processchemotaxis
U0007165biological_processsignal transduction
U0007596biological_processblood coagulation
U0009897cellular_componentexternal side of plasma membrane
U0009986cellular_componentcell surface
U0010755biological_processregulation of plasminogen activation
U0016020cellular_componentmembrane
U0019898cellular_componentextrinsic component of membrane
U0019899molecular_functionenzyme binding
U0019904molecular_functionprotein domain specific binding
U0030155biological_processregulation of cell adhesion
U0030162biological_processregulation of proteolysis
U0030377molecular_functionurokinase plasminogen activator receptor activity
U0034112biological_processpositive regulation of homotypic cell-cell adhesion
U0035579cellular_componentspecific granule membrane
U0038023molecular_functionsignaling receptor activity
U0038195biological_processurokinase plasminogen activator signaling pathway
U0042995cellular_componentcell projection
U0043066biological_processnegative regulation of apoptotic process
U0043388biological_processpositive regulation of DNA binding
U0045742biological_processpositive regulation of epidermal growth factor receptor signaling pathway
U0051917biological_processregulation of fibrinolysis
U0070161cellular_componentanchoring junction
U0090200biological_processpositive regulation of release of cytochrome c from mitochondria
U0098552cellular_componentside of membrane
U0098637cellular_componentprotein complex involved in cell-matrix adhesion
U1905370cellular_componentserine-type endopeptidase complex
U2000117biological_processobsolete negative regulation of cysteine-type endopeptidase activity
U2001243biological_processnegative regulation of intrinsic apoptotic 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_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR191-HIS197

site_idPS00524
Number of Residues21
DetailsSMB_1 Somatomedin B domain (SMB) signature. CqCdelCsyyqs.CCtDYtaeC
ChainResidueDetails
BCYS19-CYS39

site_idPS00983
Number of Residues44
DetailsLY6_UPAR Ly-6 / u-PAR domain signature. RCMqCktngd...Crve.....ECAlgqdlCrttivrlweegeelelveks....C
ChainResidueDetails
UARG2-CYS45
UGLU94-CYS147
UGLN193-CYS247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues81
DetailsDomain: {"description":"Kringle","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues23
DetailsRegion: {"description":"Binds urokinase plasminogen activator surface receptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Fuc) threonine","evidences":[{"source":"PubMed","id":"2023947","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Cleavage; by U-PA"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
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_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15861141","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
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_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22285761","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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