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Expression, Crystallization and the Three-dimensional Structure of the Catalytic Domain of Human Plasma Kallikrein: Implications for Structure-Based Design of Protease Inhibitors

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	8
Details	BINDING SITE FOR RESIDUE PO4 A 2

Chain	Residue
A	PO43
A	THR77
A	LYS78
A	LYS202
A	HOH304
A	HOH549
A	HOH632
A	HOH640

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 3

Chain	Residue
A	ASP173
A	LYS202
A	HIS203
A	ASN204
A	GLY205
A	HOH362
A	HOH549
A	HOH640
A	PO42

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 4

Chain	Residue
A	HIS91
A	GLN92
A	ARG179
A	TRP237
A	HOH635

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BEN A 1

Chain	Residue
A	ASP189
A	ALA190
A	SER195
A	SER214
A	TRP215
A	GLY219
A	GLY226
A	HOH576

---

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

---

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

Chain	Residue	Details
A	ASP189-VAL200

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	235
Details	Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3521732","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3521732","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	HIS57

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	SER195
A	GLY196

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	SER195
A	GLY193

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	HIS57

---

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	HIS57
A	GLY196

---

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	GLY193
A	HIS57

---