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1BDA

CATALYTIC DOMAIN OF HUMAN SINGLE CHAIN TISSUE PLASMINOGEN ACTIVATOR IN COMPLEX WITH DANSYL-EGR-CMK (DANSYL-GLU-GLY-ARG CHLOROMETHYL KETONE)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 2Z0 A 245
ChainResidue
AHIS57
AGLY216
AGLY219
BTRP133
BTYR163
BARG167
BASP223
ATYR99
AARG174
AASP189
AALA190
AGLY193
ASER195
ASER214
ATRP215

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 2Z0 B 245
ChainResidue
ATRP133
ATYR163
AARG167
AASP185
AASP223
BHIS57
BTYR99
BARG174
BASP189
BALA190
BGLN192
BGLY193
BSER195
BSER214
BTRP215
BGLY216
BLEU217
BGLY219

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LSAAHC
ChainResidueDetails
ALEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPLV
ChainResidueDetails
AASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues500
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"8613982","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Important for single-chain activity"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000031","evidences":[{"source":"PubMed","id":"2513186","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57
AGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

site_idMCSA1
Number of Residues4
DetailsM-CSA 798
ChainResidueDetails
AHIS57proton acceptor, proton donor
AASP102electrostatic stabiliser
AGLY193electrostatic stabiliser
ASER195electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 798
ChainResidueDetails
BHIS57proton acceptor, proton donor
BASP102electrostatic stabiliser
BGLY193electrostatic stabiliser
BSER195electrostatic stabiliser

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PDB entries from 2025-12-03

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