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2hd0

Structure of the catalytic domain of hepatitis C virus NS2

Method: X-RAY DIFFRACTION Dmax: 135.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protease NS2-3 (p23)

Hepatitis C virus

UniProt P27958

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 902–1025 Chain B； UniProt 902–1025 Fragment：protease domain of NS2 BOG octyl beta-D-glucopyranoside × 4 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K Resolution 2.28 Å R-free 0.268
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain C； UniProt 902–1025 Chain D； UniProt 902–1025 Fragment：protease domain of NS2 BOG octyl beta-D-glucopyranoside × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K Resolution 2.28 Å R-free 0.268
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain E； UniProt 902–1025 Chain F； UniProt 902–1025 Fragment：protease domain of NS2 BOG octyl beta-D-glucopyranoside × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K Resolution 2.28 Å R-free 0.268
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain G； UniProt 902–1025 Chain H； UniProt 902–1025 Fragment：protease domain of NS2 BOG octyl beta-D-glucopyranoside × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K Resolution 2.28 Å R-free 0.268
5 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain I； UniProt 902–1025 Chain J； UniProt 902–1025 Fragment：protease domain of NS2 BOG octyl beta-D-glucopyranoside × 2 DMU DECYL-BETA-D-MALTOPYRANOSIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K Resolution 2.28 Å R-free 0.268
6 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain K； UniProt 902–1025 Chain L； UniProt 902–1025 Fragment：protease domain of NS2 BOG octyl beta-D-glucopyranoside × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K Resolution 2.28 Å R-free 0.268

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 2HD0 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A1R HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX Deposited 1997-12-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1026–1205（180 aa） Fragment：PROTEASE DOMAIN
Chain C 1677–1695（19 aa） Fragment：ACTIVATION DOMAIN
Mutation：INS(ASMTGGQQMG) AT N-TERMINUS, INS(GSHHHHHH) AT C-TERMINUS Mutation：INS(KK) AT N-TERMINUS, C22S, INS(KK) AT C-TERMINUS ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 1.8 M NACL, 100 MM NA/K PHOSPHATE, 10 MM B-MERCAPTOETHANOL, 100 MM MES, PH 6.5.
Resolution 2.50 Å R-free 0.261
1A1R HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX Deposited 1997-12-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 1026–1205（180 aa） Fragment：PROTEASE DOMAIN
Chain D 1677–1695（19 aa） Fragment：ACTIVATION DOMAIN
Mutation：INS(ASMTGGQQMG) AT N-TERMINUS, INS(GSHHHHHH) AT C-TERMINUS Mutation：INS(KK) AT N-TERMINUS, C22S, INS(KK) AT C-TERMINUS ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 1.8 M NACL, 100 MM NA/K PHOSPHATE, 10 MM B-MERCAPTOETHANOL, 100 MM MES, PH 6.5.
Resolution 2.50 Å R-free 0.261
1A1R HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX Deposited 1997-12-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1026–1205（180 aa） Fragment：PROTEASE DOMAIN
Chain B 1026–1205（180 aa） Fragment：PROTEASE DOMAIN
Chain C 1677–1695（19 aa） Fragment：ACTIVATION DOMAIN
Chain D 1677–1695（19 aa） Fragment：ACTIVATION DOMAIN
Mutation：INS(ASMTGGQQMG) AT N-TERMINUS, INS(GSHHHHHH) AT C-TERMINUS Mutation：INS(ASMTGGQQMG) AT N-TERMINUS, INS(GSHHHHHH) AT C-TERMINUS Mutation：INS(KK) AT N-TERMINUS, C22S, INS(KK) AT C-TERMINUS Mutation：INS(KK) AT N-TERMINUS, C22S, INS(KK) AT C-TERMINUS ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 1.8 M NACL, 100 MM NA/K PHOSPHATE, 10 MM B-MERCAPTOETHANOL, 100 MM MES, PH 6.5.
Resolution 2.50 Å R-free 0.261
1A1V HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA Deposited 1997-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric
Chain A 1193–1657（465 aa） Fragment：HELICASE DOMAIN
Mutation：;N-TERMINAL MET, K221Q, A277G, S301L, S332P, S410A, G530E, R582W, AND A 10 RESIDUE (GSGSHHHHHH) HISTIDINE TAG ATTACHED TO THE C-TERMINUS ; Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 2.20 Å R-free 0.287
1CWX SOLUTION STRUCTURE OF THE HEPATITIS C VIRUS N-TERMINAL CAPSID PROTEIN 2-45 [C-HCV(2-45)] Deposited 1999-08-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–45（44 aa） Fragment：N-TERMINAL FRAGMENT
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.9；293 K；Ionic strength (raw mmCIF value) 0.1M NACL；Pressure AMBIENT
NMR sample composition 40% D2-TRIFLUOROETHANOL;0.01M SODIUM PHOSPHATE;0.1M NACL
Resolution not provided
1HEI STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN Deposited 1997-03-31 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1206–1656（451 aa）
Chain B 1206–1656（451 aa）
Not recorded CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；50MM CA ACETATE, 20MM NACACODYLATE PH 6.5, 8% PEG5000
Resolution 2.10 Å R-free 0.320
1JR6 Solution Structure of an Engineered Arginine-rich Subdomain 2 of the Hepatitis C Virus NS3 RNA Helicase Deposited 2001-08-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1353–1507（155 aa） Fragment：arginine-rich subdomain 2
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 75 mM KiPO4；Pressure ambient
NMR sample composition 0.6 mM, U-15N,13C; | 75 mM PHOSPHATE BUFFER; 5 mM DTT, 90%H2O, 10%D2O, 0.015% NaN3
NMR sample composition 0.6 mM, U-15N,13C; | 75 mM PHOSPHATE BUFFER; 5 mM DTT, 99%D2O, 0.015% NaN3
NMR sample composition 0.3 mM, U-15N | 75 mM PHOSPHATE BUFFER; 5 mM DTT, 90%H2O, 10%D2O, 0.015% NaN3
Resolution not provided
1N1L CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X) Deposited 2002-10-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1026–1205（180 aa） Fragment：Protease domain
Mutation：A164T ZN ZINC ION × 1 TRL {1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；Inhibitor soaked into crystal generated according to Kim et al. (1996) Cell, 87, 343-355, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K
Resolution 2.60 Å R-free 0.220
1N1L CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X) Deposited 2002-10-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1026–1205（180 aa） Fragment：Protease domain
Mutation：A164T ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；Inhibitor soaked into crystal generated according to Kim et al. (1996) Cell, 87, 343-355, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K
Resolution 2.60 Å R-free 0.220
1N1L CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X) Deposited 2002-10-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1026–1205（180 aa） Fragment：Protease domain
Chain B 1026–1205（180 aa） Fragment：Protease domain
Mutation：A164T Mutation：A164T ZN ZINC ION × 2 TRL {1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；Inhibitor soaked into crystal generated according to Kim et al. (1996) Cell, 87, 343-355, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K
Resolution 2.60 Å R-free 0.220
1ONB Solution structure of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase Deposited 2003-02-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1353–1507（155 aa） Fragment：Arginine-rich subdomain 2
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 75 mM KIPO4；Pressure ambient
NMR sample composition 0.6 mM, U-15N,13C | 90% H2O/10% D2O
NMR sample composition 0.6 mM, U-15N,13C | 99.9%D2O
Resolution not provided
1R7C NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure, Sample in 50% tfe) Deposited 2003-10-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 OF SWISS-PROT SEQUENCE P27958)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.5；293 K；Pressure ambient
NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 | H2O/TFEd2 50/50 (v/v)
Resolution not provided
1R7D NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Ensemble of 51 structures, sample in 50% tfe) Deposited 2003-10-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 of Swiss-Prot sequence P27958)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.5；293 K；Pressure ambient
NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 | H2O/TFEd2 50/50 (v/v)
Resolution not provided
1R7E NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure. Sample in 100mM SDS). Deposited 2003-10-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 OF SWISS-PROT SEQUENCE P27958)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；313 K；Pressure ambient
NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 | 100mM SDS in H2O/D2O 95/5 (v/v)
Resolution not provided
1R7F NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Ensemble of 43 structures. Sample in 100mM SDS) Deposited 2003-10-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 of Swiss-Prot sequence P27958)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；313 K；Pressure ambient
NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 | 100mM SDS in H2O/D2O 95/5 (v/v)
Resolution not provided
1R7G NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure, Sample in 100mM DPC) Deposited 2003-10-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 OF SWISS-PROT SEQUENCE P27958)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；313 K；Pressure ambient
NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 | 100mM DPC in H2O/D2O 95/5 (v/v)
Resolution not provided
1RGQ M9A HCV Protease complex with pentapeptide keto-amide inhibitor Deposited 2003-11-12 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1026–1206（181 aa） Fragment：RESIDUES 1027-1207
Chain B 1026–1206（181 aa） Fragment：RESIDUES 1027-1207
Not recorded ZN ZINC ION × 2 AKP N-(PYRAZIN-2-YLCARBONYL)LEUCYLISOLEUCYL-N~1~-{1-[2-({1-CARBOXY-2-[4-(PHOSPHONOOXY)PHENYL]ETHYL}AMINO)-1,1-DIHYDROXY-2-OXOETHYL]BUT-3-ENYL}-3-CYCLOHEXYLALANINAMIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.2M N/KPO4, 2.0M NaCl, 10mM MES, 15% glycerol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.90 Å R-free 0.312
2JXF The solution structure of HCV NS4B(40-69) Deposited 2007-11-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1751–1780（30 aa） Fragment：Non-structural protein 4B, UNP residues 1751-1780
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 1mM NS4B(40-69); 50% v/v Trifluoro Ethanol D2OH; 50% v/v H2O | 50% v/v Trifluoro Ethanol D2OH; 50% v/v H2O
Resolution not provided
2KDR Solution structure of HCV NS4B(227-254) Deposited 2009-01-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain X 1938–1965（28 aa） Fragment：UNP residues 1938-1965
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) none；Pressure ambient
NMR sample composition 2mM protein-1, 50% v/v Trifluoro Ethanol D2OH; 50% v/v H2O | 50% v/v Trifluoro Ethanol D2OH; 50% v/v H2O
Resolution not provided
2N1P Structure of the C-terminal membrane domain of HCV NS5B protein Deposited 2015-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2982–3011（30 aa） Fragment：C-terminal domain (UNP residues 2982-3011)
Mutation：C14S No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions 298 K；Pressure ambient
NMR sample composition 1.4 mM protein, 1 M [U-2H] SDS, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2O8M Crystal structure of the S139A mutant of Hepatitis C Virus NS3/4A protease Deposited 2006-12-12 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1677–1695（19 aa）
Chain D 1677–1695（19 aa）
Not recorded ZN ZINC ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1.25 to 1.5M NaCl, 0.1 M MES, .1M Na/K PO4, 5mM beta-mercaptoethanol, pH 5.6-6.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.00 Å R-free 0.228
2OBQ Discovery of the HCV NS3/4A Protease Inhibitor SCH503034. Key Steps in Structure-Based Optimization Deposited 2006-12-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1677–1695（19 aa）
Chain D 1677–1695（19 aa）
Mutation：C22S Mutation：C22S ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；The protein (NS3 complexed with KK-NS4a(21-39)-KK peptide) was at 12-15 mg/ml in 15 mM MES, pH 6.5 1 M NaCl 20 mM b-mercaptoethanol. Hanging Drops were formed by mixing 4:l protein solution with 4:l {0.75-1.0 M NaCl, 0.1M Na/K phosphate 0.1 M Mes, pH 5.8-6.1 20 mM b-mercaptoethanol} The drop was equilibrated the drops over 1 ml {(1.25-1.50 M) NaCl - 0.1M Na/K phosphate 0.1 M Mes, pH 5.6-5.8, 20 mM b-mercaptoethanol} , VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.50 Å R-free 0.264
2XI2 HCV-H77 NS5B Apo Polymerase Deposited 2010-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990
Mutation：YES SO4 SULFATE ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；MES 0.1M PH 6.5, AMMONIUM SULFATE 0.2M, PEG 5000 MONOMETHYL ETHER
Resolution 1.80 Å R-free 0.207
2XI2 HCV-H77 NS5B Apo Polymerase Deposited 2010-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990
Mutation：YES SO4 SULFATE ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；MES 0.1M PH 6.5, AMMONIUM SULFATE 0.2M, PEG 5000 MONOMETHYL ETHER
Resolution 1.80 Å R-free 0.207
2XI2 HCV-H77 NS5B Apo Polymerase Deposited 2010-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990
Mutation：YES SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；MES 0.1M PH 6.5, AMMONIUM SULFATE 0.2M, PEG 5000 MONOMETHYL ETHER
Resolution 1.80 Å R-free 0.207
2XI3 HCV-H77 NS5B Polymerase Complexed With GTP Deposited 2010-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990
Mutation：YES GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；MES 50MM PH 6.5, AMMONIUM SULFATE 0.2M, AMMONIUM ACETATE 0.25M, PEG 1000 25%-30%
Resolution 1.70 Å R-free 0.198
2XI3 HCV-H77 NS5B Polymerase Complexed With GTP Deposited 2010-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990
Mutation：YES GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；MES 50MM PH 6.5, AMMONIUM SULFATE 0.2M, AMMONIUM ACETATE 0.25M, PEG 1000 25%-30%
Resolution 1.70 Å R-free 0.198
4JZN Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-1 Deposited 2013-04-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain K 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM TRIS pH 8.0 19% PEG4000 170mM Lithium Sulfate 15% Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.05 Å R-free 0.235
4JZO Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-27 Deposited 2013-04-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain J 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；23% PEG 3350 250mM Sodium Thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.22 Å R-free 0.236
4JZO Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-27 Deposited 2013-04-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain K 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；23% PEG 3350 250mM Sodium Thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.22 Å R-free 0.236
4JZO Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-27 Deposited 2013-04-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain I 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；23% PEG 3350 250mM Sodium Thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.22 Å R-free 0.236
4JZO Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-27 Deposited 2013-04-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain L 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；23% PEG 3350 250mM Sodium Thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.22 Å R-free 0.236
4MWF Structure of Hepatitis C Virus Envelope Glycoprotein E2 core bound to broadly neutralizing antibody AR3C Deposited 2013-09-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 412–459（48 aa）
Chain D 486–645（160 aa）
Mutation：N448D, N576D Mutation：N448D, N576D NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；20% (w/v) PEG 4000, 10% (v/v) isopropanol, and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.65 Å R-free 0.270
4MWF Structure of Hepatitis C Virus Envelope Glycoprotein E2 core bound to broadly neutralizing antibody AR3C Deposited 2013-09-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 412–459（48 aa）
Chain C 486–645（160 aa）
Mutation：N448D, N576D Mutation：N448D, N576D NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；20% (w/v) PEG 4000, 10% (v/v) isopropanol, and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.65 Å R-free 0.270
4Q0X Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2 Deposited 2014-04-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 421–446（26 aa） Fragment：epitope II (UNP residues 421-446)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；0.1 M imidazole, 14% w/v PEG550 MME, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.90 Å R-free 0.285
5FGB Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC33.4 Deposited 2015-12-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 405–425（21 aa）
Not recorded GOL GLYCEROL × 2 SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；293 K；100 mM sodium citrate pH 5.2 300 mM ammonium sulfate 100 mM potassium phosphate 1 M lithium chloride
Resolution 1.65 Å R-free 0.190
5FGB Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC33.4 Deposited 2015-12-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain G 405–425（21 aa）
Not recorded GOL GLYCEROL × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；293 K；100 mM sodium citrate pH 5.2 300 mM ammonium sulfate 100 mM potassium phosphate 1 M lithium chloride
Resolution 1.65 Å R-free 0.190
5FGC Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC33.8 Deposited 2015-12-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 405–425（21 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；32% PEG 4000 100 mM Tris-HCl pH 8.5 800 mM lithium chloride Crystals obtained using heterologous microseeding.
Resolution 1.90 Å R-free 0.236

26 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_HCVH
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–128； UniProt 902–1025 Author chain B； PDBConstruct 2–128； UniProt 902–1025 Author chain C； PDBConstruct 2–128； UniProt 902–1025 Author chain D； PDBConstruct 2–128； UniProt 902–1025 Author chain E； PDBConstruct 2–128； UniProt 902–1025 Author chain F； PDBConstruct 2–128； UniProt 902–1025 Author chain G； PDBConstruct 2–128； UniProt 902–1025 Author chain H； PDBConstruct 2–128； UniProt 902–1025 Author chain I； PDBConstruct 2–128； UniProt 902–1025 Author chain J； PDBConstruct 2–128； UniProt 902–1025 Author chain K； PDBConstruct 2–128； UniProt 902–1025 Author chain L； PDBConstruct 2–128； UniProt 902–1025

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2hd0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2hd0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2hd0
Deposition date deposition_date2006-06-19
Structure title titleStructure of the catalytic domain of hepatitis C virus NS2
Keywords keywordsCysteine Protease, Dimer, Composite Active Site, Hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier42.43 Å
Radius of gyration Rg (electron density) rg_electron42.01 Å
Forward intensity I(0) i0380631000.00
Molecular weight molecular_weight167260.0 kDa
Excluded volume excluded_volume213160 ų
Envelope volume envelope_volume298580 ų
Hydration-shell volume shell_volume60927 ų
Envelope diameter envelope_diameter139.3 Å
Shell Rg shell_rg45.86 Å
Envelope Rg envelope_rg40.72 Å
Shape Rg shape_rg42.02 Å
Total Rg total_rg42.18 Å
Total atoms total_atoms11754
Residues n_residues1525
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax135.2 Å
Rg (real space) rg_real42.52 Å
Rg uncertainty (real space) rg_real_error1.07 Å
I(0) (real space) i0_real3.8060e+08
I(0) uncertainty (real space) i0_real_error6.7200e+06
Rg (reciprocal space) rg_reciprocal42.43 Å
I(0) (reciprocal space) i0_reciprocal380600000.0000
Solution quality estimate total_estimate0.8333
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.5 Å
Skewness Skewness skewness0.415
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.1850 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha116000000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.782; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.483
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 24 domains

CATH v4.4 (24 domains)

Domain ID domain_id2hd0A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0A02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0B01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0B02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0C01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0C02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0D01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0D02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0E01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0E02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0F01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0F02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0G01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0G02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0H01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0H02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0I01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0I02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0J01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0J02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0K01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0K02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
Domain ID domain_id2hd0L01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily150 — Hepatitis C virus non-structural protein NS2, N-terminal domain
Domain ID domain_id2hd0L02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily710 — Hepatitis C virus non-structural protein NS2, C-terminal domain
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8. Citations (1)

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9. Files and Curves (10)