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7E50

Crystal structure of human microplasmin in complex with kazal-type inhibitor AaTI

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU599-CYS604

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV
ChainResidueDetails
BASP735-VAL746

site_idPS00282
Number of Residues24
DetailsKAZAL_1 Kazal serine protease inhibitors family signature. CpriyMpvCgSnlktYnndCllrC
ChainResidueDetails
ACYS11-CYS34

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS603
BASP646
BSER741

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by plasminogen activator
ChainResidueDetails
BARG561

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9201958
ChainResidueDetails
BSER578

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER669

Catalytic Information from CSA
site_idMCSA1
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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