6V5T

Crystal structure of human prethrombin-2 with tryptophans replaced by 5-F-tryptophan

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005509	molecular_function	calcium ion binding
E	0005576	cellular_component	extracellular region
E	0006508	biological_process	proteolysis
E	0007596	biological_process	blood coagulation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue GOL E 301

Chain	Residue
E	HIS57
E	FTR60
E	LEU99
E	FTR148
E	FTR215

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site_id	AC2
Number of Residues	6
Details	binding site for residue SO4 E 302

Chain	Residue
E	HOH416
E	HOH459
E	ILE162
E	VAL163
E	ARG165
E	PHE181

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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
E	LEU53-CYS58

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

Chain	Residue	Details
E	ASP189-VAL200

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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
E	HIS57
E	ASP102
E	SER195

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Cleavage; by factor Xa => ECO:0000269|PubMed:34265300

Chain	Residue	Details
E	ARG15

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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:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923

Chain	Residue	Details
E	ASN60

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