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5QCN

FACTOR XIA IN COMPLEX WITH THE INHIBITOR 4-[[(1~{S})-2-[(~{E})-3-[5-chloranyl-2-(1,2,3,4-tetrazol-1-yl)phenyl]prop-2-enoyl]-5-[(3~{S})-3-ethoxycarbonylpiperidin-1-yl]carbonyl-3,4-dihydro-1~{H}-isoquinolin-1-yl]carbonylamino]benzoic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues29
Detailsbinding site for residue BVM A 301
ChainResidue
AARG39
AASP189
ACYS191
ALYS192
AGLY193
ASER195
ATHR213
ATRP215
AGLY216
AGLY218
ACYS219
ALEU41
AGLY226
AVAL227
AEDO306
AEDO307
AEDO316
AHOH406
AHOH409
AHOH433
AHOH445
AHOH498
AHIS57
AGLY113
ATYR114
ASER117
AGLN118
ATYR143
AILE151

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 302
ChainResidue
ALYS169
ALYS169
AARG170
AARG170
AARG184
AARG184

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 303
ChainResidue
AASN49
ATHR111
AVAL112
ATYR114

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 304
ChainResidue
AGLN73
ASER74
AASN153

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 305
ChainResidue
AARG24
AGLY25
ATRP27
APRO28
AILE70
ALEU71
AHOH484

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO A 306
ChainResidue
ASER81
ALEU147
AGLY216
AGLU217
AGLY218
ABVM301
AEDO307

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO A 307
ChainResidue
AGLY216
AGLU217
ABVM301
AEDO306
AHOH434
AHOH500

site_idAC8
Number of Residues6
Detailsbinding site for residue EDO A 308
ChainResidue
ASER99
AGLY100
ATYR101
ATHR177
ALYS179
AMET180

site_idAC9
Number of Residues8
Detailsbinding site for residue EDO A 309
ChainResidue
AVAL163
AGLU167
AARG170
AGLY184
ATYR184
AARG184
APRO225
AHOH401

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO A 310
ChainResidue
AASN165
AHIS178
AMET180
AILE181
AASN230
AHOH521

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO A 311
ChainResidue
AGLU26
ATRP27
ATRP137
ALYS157
AHOH438

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO A 312
ChainResidue
AGLN38
ALYS77
AGLU78
AHOH407

site_idAD4
Number of Residues4
Detailsbinding site for residue EDO A 313
ChainResidue
AILE47
ALEU239
ATHR242
AGLN243

site_idAD5
Number of Residues2
Detailsbinding site for residue EDO A 314
ChainResidue
AHIS178
AHOH440

site_idAD6
Number of Residues4
Detailsbinding site for residue EDO A 315
ChainResidue
ALYS175
AHOH447
AARG24
ASER99

site_idAD7
Number of Residues3
Detailsbinding site for residue EDO A 316
ChainResidue
ALEU41
ABVM301
AHOH496

site_idAD8
Number of Residues4
Detailsbinding site for residue EDO A 317
ChainResidue
AGLU78
AASP79
ATHR80
AGLN221

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 Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS169

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234
ChainResidueDetails
AASN72

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667, ECO:0000269|PubMed:25092234
ChainResidueDetails
AGLY113

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PDB entries from 2024-07-24

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