3i5k

Crystal structure of the NS5B polymerase from Hepatitis C Virus (HCV) strain JFH1

Method: X-RAY DIFFRACTION Dmax: 149.6 Å Quality: GOOD

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

RNA-directed RNA polymerase

Hepatitis C virus JFH-1

UniProt Q99IB8

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2443–3007 Fragment:N-terminal catalytic region, UNP residues 2443-3007 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;6 to 7% PEG20000, 0.2M NaH2PO4, pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.228
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2443–3007 Fragment:N-terminal catalytic region, UNP residues 2443-3007 PO4 PHOSPHATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;6 to 7% PEG20000, 0.2M NaH2PO4, pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.228
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 2443–3007 Fragment:N-terminal catalytic region, UNP residues 2443-3007 PO4 PHOSPHATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;6 to 7% PEG20000, 0.2M NaH2PO4, pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.228
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 2443–3007 Fragment:N-terminal catalytic region, UNP residues 2443-3007 PO4 PHOSPHATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;6 to 7% PEG20000, 0.2M NaH2PO4, pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.228

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.

31 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_HCVJF
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–565; UniProt 2443–3007 Author chain B; PDBConstruct 1–565; UniProt 2443–3007 Author chain C; PDBConstruct 1–565; UniProt 2443–3007 Author chain D; PDBConstruct 1–565; UniProt 2443–3007

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 3i5k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3i5k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3i5k
Deposition date deposition_date2009-07-05
Structure title titleCrystal structure of the NS5B polymerase from Hepatitis C Virus (HCV) strain JFH1
Keywords keywords;RdRp structure (fingers, palm, thumb domains), Apoptosis, ATP-binding, Capsid protein, Cell membrane, Disulfide bond, Endoplasmic reticulum, Envelope protein, Fusion protein, Glycoprotein, Helicase, Host-virus interaction, Hydrolase, Interferon antiviral system evasion, Lipid droplet, Lipoprotein, Membrane, Metal-binding, Mitochondrion, Multifunctional enzyme, Nucleotide-binding, Nucleotidyltransferase, Nucleus, Oncogene, Palmitate, Phosphoprotein, Protease, Ribonucleoprotein, RNA replication, RNA-binding, RNA-directed RNA polymerase, Secreted, Serine protease, SH3-binding, Thiol protease, Transcription, Transcription regulation, Transferase, Transmembrane, Viral nucleoprotein, Virion ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.28
Radius of gyration Rg (electron density) rg_electron44.70
Forward intensity I(0) i0960095000.00
Molecular weight molecular_weight253170.0 kDa
Excluded volume excluded_volume315990 ų
Envelope volume envelope_volume424700 ų
Hydration-shell volume shell_volume79042 ų
Envelope diameter envelope_diameter159.6
Shell Rg shell_rg49.94
Envelope Rg envelope_rg43.53
Shape Rg shape_rg44.66
Total Rg total_rg45.03
Total atoms total_atoms17749
Residues n_residues2264
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax149.6
Rg (real space) rg_real45.15
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real9.6010e+08
I(0) uncertainty (real space) i0_real_error1.6440e+07
Rg (reciprocal space) rg_reciprocal45.28
I(0) (reciprocal space) i0_reciprocal960200000.0000
Solution quality estimate total_estimate0.8812
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.8
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha135900000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.833

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd3i5ka1
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.8 — DNA/RNA polymerases
Superfamily Superfamily superfamilye.8.1 — DNA/RNA polymerases
Family Family familye.8.1.4 — RNA-dependent RNA-polymerase
Domain ID domain_idd3i5ka2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3i5kb1
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.8 — DNA/RNA polymerases
Superfamily Superfamily superfamilye.8.1 — DNA/RNA polymerases
Family Family familye.8.1.4 — RNA-dependent RNA-polymerase
Domain ID domain_idd3i5kb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3i5kc1
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.8 — DNA/RNA polymerases
Superfamily Superfamily superfamilye.8.1 — DNA/RNA polymerases
Family Family familye.8.1.4 — RNA-dependent RNA-polymerase
Domain ID domain_idd3i5kc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3i5kd1
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.8 — DNA/RNA polymerases
Superfamily Superfamily superfamilye.8.1 — DNA/RNA polymerases
Family Family familye.8.1.4 — RNA-dependent RNA-polymerase
Domain ID domain_idd3i5kd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)