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4DUR

The X-ray Crystal Structure of Full-Length type II Human Plasminogen

Functional Information from GO Data
ChainGOidnamespacecontents
A0002020molecular_functionprotease binding
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
A0008236molecular_functionserine-type peptidase activity
A0008285biological_processnegative regulation of cell population proliferation
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0010812biological_processnegative regulation of cell-substrate adhesion
A0019899molecular_functionenzyme binding
A0019900molecular_functionkinase binding
A0019904molecular_functionprotein domain specific binding
A0022617biological_processextracellular matrix disassembly
A0031093cellular_componentplatelet alpha granule lumen
A0034185molecular_functionapolipoprotein binding
A0042730biological_processfibrinolysis
A0043536biological_processpositive regulation of blood vessel endothelial cell migration
A0048771biological_processtissue remodeling
A0051087molecular_functionprotein-folding chaperone binding
A0051702biological_processbiological process involved in interaction with symbiont
A0051918biological_processnegative regulation of fibrinolysis
A0051919biological_processpositive regulation of fibrinolysis
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A1990405molecular_functionprotein antigen binding
A2000048biological_processnegative regulation of cell-cell adhesion mediated by cadherin
B0002020molecular_functionprotease binding
B0004175molecular_functionendopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005102molecular_functionsignaling receptor binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
B0008236molecular_functionserine-type peptidase activity
B0008285biological_processnegative regulation of cell population proliferation
B0009897cellular_componentexternal side of plasma membrane
B0009986cellular_componentcell surface
B0010812biological_processnegative regulation of cell-substrate adhesion
B0019899molecular_functionenzyme binding
B0019900molecular_functionkinase binding
B0019904molecular_functionprotein domain specific binding
B0022617biological_processextracellular matrix disassembly
B0031093cellular_componentplatelet alpha granule lumen
B0034185molecular_functionapolipoprotein binding
B0042730biological_processfibrinolysis
B0043536biological_processpositive regulation of blood vessel endothelial cell migration
B0048771biological_processtissue remodeling
B0051087molecular_functionprotein-folding chaperone binding
B0051702biological_processbiological process involved in interaction with symbiont
B0051918biological_processnegative regulation of fibrinolysis
B0051919biological_processpositive regulation of fibrinolysis
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B0072562cellular_componentblood microparticle
B1990405molecular_functionprotein antigen binding
B2000048biological_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
ATYR132-CYS145
ATYR214-CYS226
ATYR304-CYS316
ATYR406-CYS418
ATYR511-CYS524

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU599-CYS604

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV
ChainResidueDetails
AASP735-VAL746

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS603
AASP646
ASER741
BHIS603
BASP646
BSER741

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AARG117
BARG426
AASP139
AARG153
AASP413
AARG426
BARG117
BASP139
BARG153
BASP413

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by stromelysin-1
ChainResidueDetails
AGLU59
BGLU59

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Interacts with fibrin
ChainResidueDetails
AARG115
AARG117
BARG115
BARG117

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Cleavage; by stromelysin-19
ChainResidueDetails
APRO447
BPRO447

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Cleavage; by plasminogen activator
ChainResidueDetails
AARG561
BARG561

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9201958
ChainResidueDetails
ASER578
BSER578

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER669
BSER669

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:3356193, ECO:0000269|PubMed:9054441
ChainResidueDetails
ASER249
BSER249

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:3356193
ChainResidueDetails
AASN289
BASN289

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:3356193
ChainResidueDetails
ATHR346
BTHR346

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 425
ChainResidueDetails
AHIS603proton shuttle (general acid/base)
AASP646electrostatic stabiliser, modifies pKa
ASER741covalent catalysis, proton shuttle (general acid/base)
AGLY742electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 425
ChainResidueDetails
BHIS603proton shuttle (general acid/base)
BASP646electrostatic stabiliser, modifies pKa
BSER741covalent catalysis, proton shuttle (general acid/base)
BGLY742electrostatic stabiliser

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PDB entries from 2024-11-06

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