5VP9

Crystal structure of HCV NS3/4A protease in complex with AM-07, an analogue of 5172-mcP1P3

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	transformation of host cell by virus

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue 9H7 A 1201

Chain	Residue
A	GLN1041
A	GLY1137
A	SER1138
A	SER1139
A	PHE1154
A	ARG1155
A	ALA1156
A	ALA1157
A	ASP1168
A	SO41202
A	HOH1312
A	PHE1043
A	HOH1380
A	HOH1385
A	TYR1056
A	HIS1057
A	GLY1058
A	ASP1081
A	ARG1123
A	LEU1135
A	LYS1136

---

site_id	AC2
Number of Residues	8
Details	binding site for residue SO4 A 1202

Chain	Residue
A	TYR1006
A	GLN1008
A	TYR1056
A	9H71201
A	HOH1312
A	HOH1353
A	HOH1354
A	HOH1382

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 1203

Chain	Residue
A	CYS1097
A	CYS1099
A	CYS1145
A	HIS1149

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166

Chain	Residue	Details
A	HIS1057
A	ASP1081
A	SER1139

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166

Chain	Residue	Details
A	CYS1097
A	CYS1099
A	CYS1145
A	HIS1149

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Cleavage; by protease NS2 => ECO:0000255|PROSITE-ProRule:PRU01030

Chain	Residue	Details
A	ASP1003

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