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1QRZ

CATALYTIC DOMAIN OF PLASMINOGEN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0004252molecular_functionserine-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idACA
Number of Residues3
DetailsACTIVE SITE FOR CHAIN A.
ChainResidue
AASP646
AHIS603
ASER741

site_idACB
Number of Residues3
DetailsACTIVE SITE FOR CHAIN B.
ChainResidue
BASP646
BHIS603
BSER741

site_idACC
Number of Residues3
DetailsACTIVE SITE FOR CHAIN C.
ChainResidue
CASP646
CHIS603
CSER741

site_idACD
Number of Residues3
DetailsACTIVE SITE FOR CHAIN D.
ChainResidue
DASP646
DHIS603
DSER741

Functional Information from PROSITE/UniProt
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 Residues12
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS603
DHIS603
DASP646
DSER741
AASP646
ASER741
BHIS603
BASP646
BSER741
CHIS603
CASP646
CSER741

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Cleavage; by plasminogen activator
ChainResidueDetails
AARG561
BARG561
CARG561
DARG561

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9201958
ChainResidueDetails
ASER578
BSER578
CSER578
DSER578

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER669
BSER669
CSER669
DSER669

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 10460175, 9783753, 10390345
ChainResidueDetails
AHIS603
ASER741
ASER741
AASP646
AGLY742

site_idCSA2
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 10460175, 9783753, 10390345
ChainResidueDetails
BHIS603
BSER741
BSER741
BASP646
BGLY742

site_idCSA3
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 10460175, 9783753, 10390345
ChainResidueDetails
CHIS603
CSER741
CSER741
CASP646
CGLY742

site_idCSA4
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 10460175, 9783753, 10390345
ChainResidueDetails
DHIS603
DSER741
DSER741
DASP646
DGLY742

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

site_idMCSA3
Number of Residues4
DetailsM-CSA 425
ChainResidueDetails
CHIS603proton shuttle (general acid/base)
CASP646electrostatic stabiliser, modifies pKa
CSER741covalent catalysis, proton shuttle (general acid/base)
CGLY742electrostatic stabiliser

site_idMCSA4
Number of Residues4
DetailsM-CSA 425
ChainResidueDetails
DHIS603proton shuttle (general acid/base)
DASP646electrostatic stabiliser, modifies pKa
DSER741covalent catalysis, proton shuttle (general acid/base)
DGLY742electrostatic stabiliser

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PDB entries from 2024-10-09

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