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1XX9

Crystal Structure of the FXIa Catalytic Domain in Complex with EcotinM84R

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
C0005515molecular_functionprotein binding
C0006952biological_processdefense response
C0010466biological_processnegative regulation of peptidase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0042803molecular_functionprotein homodimerization activity
D0004867molecular_functionserine-type endopeptidase inhibitor activity
D0005515molecular_functionprotein binding
D0006952biological_processdefense response
D0010466biological_processnegative regulation of peptidase activity
D0030288cellular_componentouter membrane-bounded periplasmic space
D0042597cellular_componentperiplasmic space
D0042803molecular_functionprotein homodimerization activity
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 Residues2
DetailsSITE: Reactive bond
ChainResidueDetails
CARG84
DARG84
ASER195
BHIS57
BASP102
BSER195

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS170
BLYS170

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234
ChainResidueDetails
AASN73
BASN73

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667, ECO:0000269|PubMed:25092234
ChainResidueDetails
AASN113
BASN113

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
AASP102
ASER195
AGLY193
AHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

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

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PDB entries from 2024-10-16

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