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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4A5T

STRUCTURAL BASIS FOR THE CONFORMATIONAL MODULATION

Functional Information from GO Data
ChainGOidnamespacecontents
S0002020molecular_functionprotease binding
S0004175molecular_functionendopeptidase activity
S0004252molecular_functionserine-type endopeptidase activity
S0005102molecular_functionsignaling receptor binding
S0005515molecular_functionprotein binding
S0005576cellular_componentextracellular region
S0005615cellular_componentextracellular space
S0005886cellular_componentplasma membrane
S0006508biological_processproteolysis
S0007596biological_processblood coagulation
S0007599biological_processhemostasis
S0008233molecular_functionpeptidase activity
S0008236molecular_functionserine-type peptidase activity
S0008285biological_processnegative regulation of cell population proliferation
S0009897cellular_componentexternal side of plasma membrane
S0009986cellular_componentcell surface
S0010812biological_processnegative regulation of cell-substrate adhesion
S0016485biological_processprotein processing
S0016787molecular_functionhydrolase activity
S0019899molecular_functionenzyme binding
S0019900molecular_functionkinase binding
S0019904molecular_functionprotein domain specific binding
S0022617biological_processextracellular matrix disassembly
S0031012cellular_componentextracellular matrix
S0031093cellular_componentplatelet alpha granule lumen
S0034185molecular_functionapolipoprotein binding
S0042246biological_processtissue regeneration
S0042730biological_processfibrinolysis
S0043536biological_processpositive regulation of blood vessel endothelial cell migration
S0045445biological_processmyoblast differentiation
S0046716biological_processmuscle cell cellular homeostasis
S0048771biological_processtissue remodeling
S0051087molecular_functionprotein-folding chaperone binding
S0051702biological_processbiological process involved in interaction with symbiont
S0051918biological_processnegative regulation of fibrinolysis
S0051919biological_processpositive regulation of fibrinolysis
S0060707biological_processtrophoblast giant cell differentiation
S0060716biological_processlabyrinthine layer blood vessel development
S0070062cellular_componentextracellular exosome
S0071674biological_processmononuclear cell migration
S0072562cellular_componentblood microparticle
S0098685cellular_componentSchaffer collateral - CA1 synapse
S0098978cellular_componentglutamatergic synapse
S0099183biological_processtrans-synaptic signaling by BDNF, modulating synaptic transmission
S1990405molecular_functionprotein antigen binding
S2000048biological_processnegative regulation of cell-cell adhesion mediated by cadherin
Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. YCRNpdndpqgpWC
ChainResidueDetails
STYR132-CYS145
STYR214-CYS226
STYR304-CYS316
STYR406-CYS418
STYR511-CYS524
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
SLEU599-CYS604
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV
ChainResidueDetails
SASP735-VAL746
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues77
DetailsPeptide: {"description":"Activation peptide","featureId":"PRO_0000028055"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues78
DetailsDomain: {"description":"PAN","evidences":[{"source":"PROSITE-ProRule","id":"PRU00315","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues78
DetailsDomain: {"description":"Kringle 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues78
DetailsDomain: {"description":"Kringle 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues77
DetailsDomain: {"description":"Kringle 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues77
DetailsDomain: {"description":"Kringle 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues79
DetailsDomain: {"description":"Kringle 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues227
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues39
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsSite: {"description":"Cleavage; by stromelysin-1"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsSite: {"description":"Interacts with fibrin"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Cleavage; by plasminogen activator"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"9201958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) serine","featureId":"CAR_000016","evidences":[{"source":"PubMed","id":"3356193","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9054441","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000017","evidences":[{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3356193","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","featureId":"CAR_000018","evidences":[{"source":"PubMed","id":"3356193","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 425
ChainResidueDetails

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PDB entries from 2025-10-29

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