Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1BUI

Structure of the ternary microplasmin-staphylokinase-microplasmin complex: a proteinase-cofactor-substrate complex in action

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0005576cellular_componentextracellular region
C0031639biological_processplasminogen activation
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 0GJ A 246
ChainResidue
ACYS191
AGLN192
AGLY193
ASER195
ASER214
ATRP215
AGLY216
AGLY219
BLYS10
CHIS43
AHIS57
AASP189
ASER190

site_idASA
Number of Residues3
DetailsCATALYTIC SITE OF CHAIN A
ChainResidue
ASER195
AHIS57
AASP102

site_idASB
Number of Residues3
DetailsCATALYTIC SITE OF CHAIN B
ChainResidue
BSER195
BHIS57
BASP102

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
ASER195
BHIS57
BASP102
BSER195

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by plasminogen activator
ChainResidueDetails
AARG15
BARG15

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9201958
ChainResidueDetails
ASER32
BSER32

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER125
BSER125

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
BASP102
BSER195
BGLY193
BHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

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 425
ChainResidueDetails
AHIS57proton shuttle (general acid/base)
AASP102electrostatic stabiliser, modifies pKa
ASER195covalent catalysis, proton shuttle (general acid/base)
AGLY196electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 425
ChainResidueDetails
BHIS57proton shuttle (general acid/base)
BASP102electrostatic stabiliser, modifies pKa
BSER195covalent catalysis, proton shuttle (general acid/base)
BGLY196electrostatic stabiliser

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon