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7CJ1

The crystal structure of FXIa serine protease domain in complex with benzamidine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0004252molecular_functionserine-type endopeptidase activity
D0006508biological_processproteolysis
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. DAckGDSGGPLS
ChainResidueDetails
AASP189-SER198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
DHIS57
DASP102
DSER195
AASP102
ASER195
BHIS57
BASP102
BSER195
CHIS57
CASP102
CSER195

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ALYS170
BLYS170
CLYS170
DLYS170

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234
ChainResidueDetails
AGLN73
BGLN73
CGLN73
DGLN73

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667, ECO:0000269|PubMed:25092234
ChainResidueDetails
AGLN113
BGLN113
CGLN113
DGLN113

226707

PDB entries from 2024-10-30

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