4nlx

Poliovirus Polymerase - G289A/C290V Loop Mutant

Method: X-RAY DIFFRACTION Dmax: 71.3 Å Quality: EXCELLENT

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

RNA-directed RNA polymerase 3D-POL

Human poliovirus 1

UniProt P03300

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 1749–2209 Mutation:G289A, C290V, L446D, 455D Non-standard monomer:Yes (specific site not provided by mmCIF) ACY ACETIC ACID × 5 1PE PENTAETHYLENE GLYCOL × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;289 K;Grown in sodium acetate, cacodylate, DTT. Transferred to 250 mM sodium acetate, 30% (w/v) PEG-400, 0.1 M cacodylic acid and 2 mM DTT, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.60 Å R-free 0.236

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.

80 other PDB entries and 250 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_POL1M
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–461; UniProt 1749–2209

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 4nlx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4nlx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4nlx
Deposition date deposition_date2013-11-14
Structure title titlePoliovirus Polymerase - G289A/C290V Loop Mutant
Keywords keywordspolymerase, RNA dependent RNA polymerase, RdRP, virus, Viral Protein, hydrolase; Viral Protein, hydrolase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.21
Radius of gyration Rg (electron density) rg_electron23.08
Forward intensity I(0) i046076700.00
Molecular weight molecular_weight53621.0 kDa
Excluded volume excluded_volume67495 ų
Envelope volume envelope_volume82349 ų
Hydration-shell volume shell_volume29077 ų
Envelope diameter envelope_diameter75.6
Shell Rg shell_rg30.65
Envelope Rg envelope_rg22.77
Shape Rg shape_rg23.08
Total Rg total_rg23.98
Total atoms total_atoms3759
Residues n_residues458
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 dmax71.3
Rg (real space) rg_real23.99
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real4.6080e+07
I(0) uncertainty (real space) i0_real_error5.3470e+05
Rg (reciprocal space) rg_reciprocal24.04
I(0) (reciprocal space) i0_reciprocal46080000.0000
Solution quality estimate total_estimate0.9091
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.4
Skewness Skewness skewness-0.008
Kurtosis Kurtosis kurtosis-0.602
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12780000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4nlxa_
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

CATH v4.4 (2 domains)

Domain ID domain_id4nlxA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily270 — Reverse transcriptase/Diguanylate cyclase domain
Domain ID domain_id4nlxA03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology960 — Mitochondrial Import Receptor Subunit Tom20; Chain A
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)