1n1l

CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X)

Method: X-RAY DIFFRACTION D_max: 75.6 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

HCV NS3 SERINE PROTEASE

Hepatitis C virus

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1026–1205	Fragment：Protease domain Mutation：A164T	NS4A COFACTOR × 1 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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1026–1205	Fragment：Protease domain Mutation：A164T	NS4A COFACTOR × 1 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
3	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1026–1205 Chain B； UniProt 1026–1205	Fragment：Protease domain Mutation：A164T	NS4A COFACTOR × 2 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

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 1N1L	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 oligomeric state 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 oligomeric state 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 mutation/modification Different oligomeric state 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
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 mutation/modification 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
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 902–1025（124 aa） Fragment：protease domain of NS2 Chain B 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	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
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 902–1025（124 aa） Fragment：protease domain of NS2 Chain D 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	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
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 902–1025（124 aa） Fragment：protease domain of NS2 Chain F 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	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
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 902–1025（124 aa） Fragment：protease domain of NS2 Chain H 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	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
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain I 902–1025（124 aa） Fragment：protease domain of NS2 Chain J 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	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
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain K 902–1025（124 aa） Fragment：protease domain of NS2 Chain L 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	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
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 mutation/modification 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 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 41 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 11–190； UniProt 1026–1205 Author chain B； PDBConstruct 11–190； UniProt 1026–1205

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1n1l
Deposition date deposition_date	2002-10-18
Structure title title	CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X)
Keywords keywords	VIRAL PROTEIN, SERINE PROTEASE, NONSTRUCTURAL PROTEINS, COFACTOR PEPTIDE, HELICASE, INHIBITOR; VIRAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	23.09 Å
Radius of gyration Rg (electron density) rg_electron	22.35 Å
Forward intensity I(0) i0	27224700.00
Molecular weight molecular_weight	39558.0 kDa
Excluded volume excluded_volume	49524 Å³
Envelope volume envelope_volume	59153 Å³
Hydration-shell volume shell_volume	22461 Å³
Envelope diameter envelope_diameter	77.8 Å
Shell Rg shell_rg	28.68 Å
Envelope Rg envelope_rg	22.55 Å
Shape Rg shape_rg	22.35 Å
Total Rg total_rg	23.16 Å
Total atoms total_atoms	2763
Residues n_residues	370
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	75.6 Å
Rg (real space) rg_real	23.10 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	2.7220e+07
I(0) uncertainty (real space) i0_real_error	3.9250e+05
Rg (reciprocal space) rg_reciprocal	23.10 Å
I(0) (reciprocal space) i0_reciprocal	27220000.0000
Solution quality estimate total_estimate	0.8916
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.4 Å
Skewness Skewness skewness	0.337
Kurtosis Kurtosis kurtosis	-0.481
Angular range angular_range	— – 0.3450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8610000.0000
Real-space data points n_real_points	66
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.975

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	HCV NS3 SERINE PROTEASE
Molecular weight formula_weight	21045.0 kDa
Mutation mutation	A164T
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2870

ASMTGGQQMGAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVTKAVDFIPVENLETTMRGSHHHHHH

来源 Source

来源生物 organism	Hepatitis C virus
NCBI Class编号 ncbi_taxonomy_id	11103
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	NS4A COFACTOR
Molecular weight formula_weight	2394.0 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

KKGSVVIVGRIVLSGKPAIIPKK

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	{1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTER
Molecular weight formula_weight	433.6 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	107

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1n1l.1
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.3 — Viral proteases

Domain ID domain_id	d1n1l.2
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.3 — Viral proteases

CATH v4.4 (4 domains)

Domain ID domain_id	1n1lA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	1n1lA02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1n1lB01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	1n1lB02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

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8. Citations (1)

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Unit-cell length a length_a	225.450 Å
Unit-cell length b length_b	225.450 Å
Unit-cell length c length_c	75.890 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	36

Space group space_group	H 3 2
Space-group number int_tables_number	155
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1851
R_work r_work	0.1832
R_free r_free	0.2195

fit	/app/data/saxs_computation/n1/1n1l/1n1l.fit
pddf	/app/data/pr_computation/n1/1n1l/1n1l.pr.out
profile	/app/data/saxs_computation/n1/1n1l/1n1l.dat

CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X)

1. Protein Identity and Related Structures Protein Identity & Related Structures

HCV NS3 SERINE PROTEASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)