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5E2O

FACTOR XIA IN COMPLEX WITH THE INHIBITOR 4-[(N-{(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl}-L-phenylalanyl)amino]benzoic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue 5JM A 301
ChainResidue
ALEU41
AASP194
ASER195
ATHR213
ATRP215
AGLY216
AGLY218
ACYS219
AGLY226
AVAL227
AEDO304
AHIS57
AEDO308
AHOH402
AHOH493
ATYR143
AILE151
AASP189
AALA190
ACYS191
ALYS192
AGLY193

site_idAC2
Number of Residues11
Detailsbinding site for residue SO4 A 302
ChainResidue
AVAL23
AARG24
AGLY25
AGLU26
ATRP27
AILE70
ALEU71
ALEU155
AHOH412
AHOH415
AHOH428

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG170
AARG170
AARG184
AARG184

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 304
ChainResidue
A5JM301
AEDO308
AEDO309
AHOH557

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 305
ChainResidue
AASN49
ATHR111
AVAL112
AGLY113
ATYR114

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 306
ChainResidue
AGLN73
ASER74
AASN153

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 307
ChainResidue
AARG24
ASER99
ALYS175
AHOH456
AHOH465

site_idAC8
Number of Residues8
Detailsbinding site for residue EDO A 308
ChainResidue
ASER81
AGLY216
AGLU217
AGLY218
A5JM301
AEDO304
AEDO309
AHOH479

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO A 309
ChainResidue
ATRP215
AGLY216
AGLU217
AEDO304
AEDO308
AHOH439

site_idAD1
Number of Residues2
Detailsbinding site for residue EDO A 310
ChainResidue
ATHR177
AHIS178

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO A 311
ChainResidue
ASER99
AGLY100
ATYR101
ATHR177
ALYS179

site_idAD3
Number of Residues9
Detailsbinding site for residue EDO A 312
ChainResidue
AVAL163
AGLU167
AARG170
AGLY184
ATYR184
AARG184
AGLU223
APRO225
AHOH408

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-SER200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues235
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1998667","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25092234","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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