Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6BQJ

CRYSTAL STRUCTURE OF HEPATIS C VIRUS PROTEASE (NS3) COMPLEXED WITH TRIPEPTIDIC ACYL SULFONAMIDE INHIBITOR (COMPOUND 16)

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
B	0006508	biological_process	proteolysis
B	0008236	molecular_function	serine-type peptidase activity
B	0019087	biological_process	transformation of host cell by virus
C	0006508	biological_process	proteolysis
C	0008236	molecular_function	serine-type peptidase activity
C	0019087	biological_process	transformation of host cell by virus

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue Z1B A 301

Chain	Residue
A	TYR56
A	SER139
A	PHE154
A	ARG155
A	ALA156
A	ALA157
A	CYS159
A	ASP168
A	HOH440
A	HOH449
A	HOH456
A	HIS57
A	HOH486
A	VAL78
A	ASP79
A	ASP81
A	ILE132
A	LEU135
A	GLY137
A	SER138

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 302

Chain	Residue
A	CYS97
A	CYS99
A	CYS145
A	CL303

site_id	AC3
Number of Residues	3
Details	binding site for residue CL A 303

Chain	Residue
A	THR98
A	CYS99
A	ZN302

site_id	AC4
Number of Residues	4
Details	binding site for residue ACT A 304

Chain	Residue
A	ARG155
A	ILE170
A	SER174
A	HOH494

site_id	AC5
Number of Residues	1
Details	binding site for residue ACT A 305

Chain	Residue
A	GLN86

site_id	AC6
Number of Residues	17
Details	binding site for residue Z1B B 301

Chain	Residue
B	TYR56
B	HIS57
B	VAL78
B	ASP79
B	ASP81
B	ARG123
B	LEU135
B	GLY137
B	SER138
B	SER139
B	PHE154
B	ARG155
B	ALA156
B	ALA157
B	ASP168
B	HOH442
B	HOH443

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN B 302

Chain	Residue
B	CYS97
B	CYS99
B	CYS145
B	CL303

site_id	AC8
Number of Residues	3
Details	binding site for residue CL B 303

Chain	Residue
B	THR98
B	CYS99
B	ZN302

site_id	AC9
Number of Residues	2
Details	binding site for residue ACT B 304

Chain	Residue
B	ARG155
B	SER174

site_id	AD1
Number of Residues	18
Details	binding site for residue Z1B C 301

Chain	Residue
C	TYR56
C	HIS57
C	ASP81
C	ARG123
C	ILE132
C	LEU135
C	GLY137
C	SER138
C	SER139
C	PHE154
C	ARG155
C	ALA156
C	ALA157
C	CYS159
C	ASP168
C	HOH414
C	HOH453
C	HOH456

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN C 302

Chain	Residue
C	CYS97
C	CYS99
C	CYS145
C	CL303

site_id	AD3
Number of Residues	3
Details	binding site for residue CL C 303

Chain	Residue
C	THR98
C	CYS99
C	ZN302

site_id	AD4
Number of Residues	5
Details	binding site for residue ACT C 304

Chain	Residue
A	PRO129
C	ARG130
C	PRO131
C	VAL163
C	HOH496

site_id	AD5
Number of Residues	3
Details	binding site for residue ACT C 305

Chain	Residue
B	HOH464
C	HIS110
C	HOH418

site_id	AD6
Number of Residues	3
Details	binding site for residue ACT C 306

Chain	Residue
C	ARG155
C	PRO171
C	SER174

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, ECO:0000269\|PubMed:8386278, ECO:0000305\|PubMed:8861917

Chain	Residue	Details
A	HIS57
B	HIS57
C	HIS57

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255\|PROSITE-ProRule:PRU01166, ECO:0000305\|PubMed:8861917

Chain	Residue	Details
A	ASP81
B	ASP81
C	ASP81

site_id	SWS_FT_FI3
Number of Residues	3
Details	ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255\|PROSITE-ProRule:PRU01166, ECO:0000269\|PubMed:8248148, ECO:0000269\|PubMed:8386278, ECO:0000305\|PubMed:8861917

Chain	Residue	Details
A	SER139
B	SER139
C	SER139

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01166, ECO:0000269\|PubMed:21507982, ECO:0007744\|PDB:1A1R, ECO:0007744\|PDB:1N1L, ECO:0007744\|PDB:1RGQ, ECO:0007744\|PDB:2A4R, ECO:0007744\|PDB:2F9V, ECO:0007744\|PDB:2O8M, ECO:0007744\|PDB:2OBQ, ECO:0007744\|PDB:2OC0, ECO:0007744\|PDB:2OC1, ECO:0007744\|PDB:2OC7, ECO:0007744\|PDB:2OC8, ECO:0007744\|PDB:2OIN, ECO:0007744\|PDB:2XNI

Chain	Residue	Details
A	CYS97
A	CYS99
B	CYS97
B	CYS99
C	CYS97
C	CYS99

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01166, ECO:0000269\|PubMed:21507982, ECO:0007744\|PDB:1N1L, ECO:0007744\|PDB:1RGQ, ECO:0007744\|PDB:2A4R, ECO:0007744\|PDB:2F9V, ECO:0007744\|PDB:2O8M, ECO:0007744\|PDB:2OBQ, ECO:0007744\|PDB:2OC0, ECO:0007744\|PDB:2OC1, ECO:0007744\|PDB:2OC7, ECO:0007744\|PDB:2OC8, ECO:0007744\|PDB:2OIN, ECO:0007744\|PDB:2XNI

Chain	Residue	Details
A	CYS145
B	CYS145
C	CYS145

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01166, ECO:0000269\|PubMed:21507982

Chain	Residue	Details
A	HIS149
B	HIS149
C	HIS149

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
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	4
Details	M-CSA 776

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

site_id	MCSA3
Number of Residues	4
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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)