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6TWB

Crystal Structure of the Catalytic Domain of Coagulation Factor XIa in Complex with Double Bridged Peptide F19

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
H0004252molecular_functionserine-type endopeptidase activity
H0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue NH4 A 301
ChainResidue
AARG24
ALYS175

site_idAC2
Number of Residues1
Detailsbinding site for residue NH4 A 302
ChainResidue
AHIS178

site_idAC3
Number of Residues2
Detailsbinding site for residue NH4 B 101
ChainResidue
BCSA1
BVAL2

site_idAC4
Number of Residues4
Detailsbinding site for Di-peptide CSA B 1 and VAL B 2
ChainResidue
AGLN118
BASN3
BCYS7
BNH4101

site_idAC5
Number of Residues10
Detailsbinding site for Di-peptide CSA B 1 and CYS B 7
ChainResidue
ALYS192
AGLY218
BVAL2
BASN3
BILE4
BMET5
BCSA6
BARG8
BCYS9
BNH4101

site_idAC6
Number of Residues14
Detailsbinding site for Di-peptide MET B 5 and CSA B 6
ChainResidue
AHIS57
AALA97
AGLU98
ATYR171
AHIS174
ASER214
ATRP215
AGLY216
AGLU217
BASN3
BILE4
BCYS7
BARG8
BCYS9

site_idAC7
Number of Residues12
Detailsbinding site for Di-peptide CSA B 6 and CYS B 9
ChainResidue
AHIS57
AALA97
ALYS192
ASER195
ASER214
BASN3
BILE4
BMET5
BCYS7
BARG8
BPRO10
BNH211

site_idAC8
Number of Residues11
Detailsbinding site for Di-peptide CSA B 6 and CYS B 7
ChainResidue
AHIS57
AALA97
ALYS192
ASER214
AGLY218
BCSA1
BASN3
BILE4
BMET5
BARG8
BCYS9

site_idAC9
Number of Residues6
Detailsbinding site for Di-peptide PRO B 10 and NH2 B 11
ChainResidue
AARG39
ALEU41
ALYS192
ASER195
AHOH401
BCYS9

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 Residues4
DetailsACT_SITE: Charge relay system
ChainResidueDetails
ALYS107
ALYS157
HLYS467
HLYS516

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLN221
HGLN583

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234
ChainResidueDetails
ALYS126
HLYS486

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667, ECO:0000269|PubMed:25092234
ChainResidueDetails
ACYS168
HCYS527

219869

PDB entries from 2024-05-15

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