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5E2P

FACTOR XIA IN COMPLEX WITH THE INHIBITOR N-[(1S)-1-benzyl-2-[2-[5-chloro-2-(tetrazol-1-yl)phenyl]ethylamino]-2-oxo-ethyl]-4-hydroxy-2-oxo-1H-quinoline-6-carboxamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue 7P0 A 301
ChainResidue
AARG39
ALYS192
AGLY193
AASP194
ASER195
ATHR213
ASER214
ATRP215
AGLY216
AGLY218
ACYS219
AHIS40
AGLY226
AVAL227
AEDO303
AEDO307
AEDO310
AHOH441
AHOH466
AHOH515
AHOH516
ALEU41
AHIS57
ATYR143
AILE151
AASP189
AALA190
ACYS191

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 302
ChainResidue
AARG170
AARG170
AARG184
AARG184

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 303
ChainResidue
ALYS192
A7P0301
AEDO307
AEDO310
AHOH510

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 304
ChainResidue
AASN49
AVAL112
AGLY113
ATYR114

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 305
ChainResidue
AARG24
ASER99
AGLY173
ALYS175
AHOH431
AHOH445
AHOH485

site_idAC6
Number of Residues8
Detailsbinding site for residue EDO A 306
ChainResidue
AARG24
AGLY25
ATRP27
APRO28
AILE70
ALEU71
ASER117
AHOH424

site_idAC7
Number of Residues7
Detailsbinding site for residue EDO A 307
ChainResidue
ASER81
AGLY216
AGLU217
AGLY218
A7P0301
AEDO303
AEDO308

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO A 308
ChainResidue
AGLU98
AHIS174
ATRP215
AGLY216
AGLU217
AEDO307
AHOH521

site_idAC9
Number of Residues1
Detailsbinding site for residue EDO A 309
ChainResidue
AHIS178

site_idAD1
Number of Residues7
Detailsbinding site for residue EDO A 310
ChainResidue
AHIS57
ASER214
ATRP215
A7P0301
AEDO303
AEDO312
AHOH521

site_idAD2
Number of Residues7
Detailsbinding site for residue EDO A 311
ChainResidue
AGLU167
AARG170
AGLY184
ATYR184
AARG184
APRO225
AHOH403

site_idAD3
Number of Residues7
Detailsbinding site for residue EDO A 312
ChainResidue
ATYR94
AMET96
AALA97
AGLU98
ASER117
AEDO310
AHOH453

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

238895

PDB entries from 2025-07-16

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