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7E50

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0030414molecular_functionpeptidase inhibitor activity
A0044470biological_processvenom-mediated suppression of blood coagulation
A0050688biological_processregulation of defense response to virus
A0090729molecular_functiontoxin activity
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 Residues53
DetailsDomain: {"description":"Kazal-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Reactive bond","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues227
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"9201958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

247536

PDB entries from 2026-01-14

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