2OC1

Structure of the HCV NS3/4A Protease Inhibitor CVS4819

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008236	molecular_function	serine-type peptidase activity
A	0019087	biological_process	symbiont-mediated transformation of host cell
C	0006508	biological_process	proteolysis
C	0008236	molecular_function	serine-type peptidase activity
C	0019087	biological_process	symbiont-mediated transformation of host cell

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 901

Chain	Residue
A	CYS97
A	CYS99
A	CYS145
A	HOH1009

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 902

Chain	Residue
C	CYS97
C	CYS99
C	CYS145
C	HOH903

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HU2 A 999

Chain	Residue
A	THR42
A	HIS57
A	ARG123
A	ILE132
A	LYS136
A	GLY137
A	SER138
A	SER139
A	ARG155
A	ALA156
A	ALA157
A	ASP168
A	GLN41

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8386278","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8861917","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8861917","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8248148","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8386278","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8861917","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21507982","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Cleavage; by protease NS2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01030","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	22
Details	Region: {"description":"NS3-binding","evidences":[{"source":"PubMed","id":"7769699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8861917","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1rgq

Chain	Residue	Details
A	ASP81
A	SER139
A	GLY137
A	HIS57

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1rgq

Chain	Residue	Details
C	ASP81
C	SER139
C	GLY137
C	HIS57

---

site_id	MCSA1
Number of Residues
Details	M-CSA 776

Chain	Residue	Details
A	HIS57	proton shuttle (general acid/base)
A	ASP81	electrostatic stabiliser
A	GLY137	electrostatic stabiliser
A	SER139	covalently attached, electrostatic stabiliser

---

site_id	MCSA2
Number of Residues
Details	M-CSA 776

Chain	Residue	Details
C	HIS57	proton shuttle (general acid/base)
C	ASP81	electrostatic stabiliser
C	GLY137	electrostatic stabiliser
C	SER139	covalently attached, electrostatic stabiliser

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