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4NA8

Factor XIa in complex with the inhibitor 5-aminocarbonyl-2-[3-[(2s,4r)-6-carbamimidoyl-4-methyl-4-phenyl-2,3-dihydro-1h-quinolin-2-yl]phenyl]benzoic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 1T6 A 301
ChainResidue
AARG39
ALYS192
AGLY193
ASER195
ASER214
ATRP215
AGLY216
AGLY218
ACYS219
AGLY226
AHOH405
AHIS40
AHOH471
AHOH496
ALEU41
ACYS42
AHIS57
ATHR115
AILE151
AASP189
AALA190

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
ALYS169
ALYS169
AARG170
AARG170
AARG184
AARG184

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AASN49
ATHR111
AVAL112
AASN113
ATYR114

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AARG24
AGLY25
AGLU26
ATRP27
AILE70
ALEU71
ALEU155

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

249697

PDB entries from 2026-02-25

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