6O1S

Structure of human plasma kallikrein protease domain with inhibitor

Replaces:  5TZ9

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue PO4 E 801

Chain	Residue
E	HIS472
E	GLN473
E	ARG560
E	HOH1027

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site_id	AC2
Number of Residues	6
Details	binding site for residue EDO E 802

Chain	Residue
E	HOH1003
E	TRP402
E	GLN405
E	GLY450
E	ILE451
E	HOH973

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site_id	AC3
Number of Residues	19
Details	binding site for residue 7SD E 803

Chain	Residue
E	HIS434
E	GLY480
E	TYR555
E	MET561
E	ASP572
E	ALA573
E	CYS574
E	SER578
E	THR596
E	SER597
E	TRP598
E	GLY599
E	GLY601
E	CYS602
E	ASP629
E	HOH972
E	HOH980
E	HOH989
E	HOH1009

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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	LEU430-CYS435

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

Chain	Residue	Details
E	ASP572-VAL583

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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	HIS434
E	ASP483
E	SER578

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732

Chain	Residue	Details
E	GLU396
E	GLU494

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732

Chain	Residue	Details
E	GLU453

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