3NXP

Crystal structure of human prethrombin-1

Functional Information from GO Data

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

Functional Information from PROSITE/UniProt

site_id	PS00021
Number of Residues	14
Details	KRINGLE_1 Kringle domain signature. FCRNpdgdeegvWC

Chain	Residue	Details
A	PHE218-CYS231

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

Chain	Residue	Details
A	LEU453-CYS458

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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
A	ASP589-VAL600

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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	HIS457
A	ASP502
A	SER595

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Cleavage; by factor Xa => ECO:0000269|PubMed:34265300

Chain	Residue	Details
A	ALA271
A	ARG320

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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
A	ASN460

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