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3UIR

Crystal structure of the plasmin-textilinin-1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004867molecular_functionserine-type endopeptidase inhibitor activity
C0005576cellular_componentextracellular region
C0035899biological_processsuppression of blood coagulation in another organism
C0090729molecular_functiontoxin activity
D0004867molecular_functionserine-type endopeptidase inhibitor activity
D0005576cellular_componentextracellular region
D0035899biological_processsuppression of blood coagulation in another organism
D0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 801
ChainResidue
BARG712
BTYR713

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 101
ChainResidue
DTHR49
DLYS50
DGLU51

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

site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FiyGGCegnannFitkeeC
ChainResidueDetails
CPHE35-CYS53

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Reactive bond for trypsin => ECO:0000250
ChainResidueDetails
CARG17
DARG17
ASER741
BHIS603
BASP646
BSER741

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by plasminogen activator
ChainResidueDetails
AARG561
BARG561

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9201958
ChainResidueDetails
ASER578
BSER578

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER669
BSER669

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 2024-06-12

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