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1ZPZ

Factor XI catalytic domain complexed with N-((R)-1-(4-bromophenyl)ethyl)urea-Asn-Val-Arg-alpha-ketothiazole

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AGLY46
AASN47
ATYR114
APRO121
AARG171
AARG185
AHOH965

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE BUK A 900
ChainResidue
AASN113
ATHR115
AGLN118
AASP189
AALA190
ACYS191
ALYS192
AGLY193
AASP194
ASER195
ASER214
ATRP215
AGLY216
AGLY218
AGLY226
AHIS57
AGLU98

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 Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS170

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
AASN73

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
AASN113

218853

PDB entries from 2024-04-24

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