6TWC

Crystal Structure of the Catalytic Domain of the Coagulation Factor XIa in Complex with Double Bridged Peptide F21

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue ACN C 101

Chain	Residue
A	LEU147
A	LYS192
C	THR1
C	CYS2
C	ASN4
C	CYS8

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site_id	AC2
Number of Residues	6
Details	binding site for residue ACN C 102

Chain	Residue
C	MET6
C	CYS7
C	CYS10
A	HIS57
A	ALA97
A	SER214

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Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC

Chain	Residue	Details
A	LEU53-CYS58

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site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAckGDSGGPLS

Chain	Residue	Details
A	ASP189-SER200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Charge relay system

Chain	Residue	Details
A	HIS57
A	ASP102
A	SER195

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	LYS169

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234

Chain	Residue	Details
A	ASN72

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site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667, ECO:0000269|PubMed:25092234

Chain	Residue	Details
A	GLY113

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