4k4w

Poliovirus polymerase elongation complex (r5+2_form)

Method: X-RAY DIFFRACTION Dmax: 134.4 Å Quality: REASONABLE

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–RNA Monomer Protein × 1 RNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 1749–2209 Fragment:unp residues 1749-2209 Mutation:L446D, C290A ;RNA (5'-R(P*GP*GP*GP*AP*GP*AP*UP*GP*AP*AP*AP*GP*UP*CP*UP*CP*CP*AP*GP*GP*UP*CP*UP*CP*UP*CP*UP*CP*GP*UP*CP*GP*AP*AP*A)-3') ; × 1 ;RNA (5'-R(*UP*GP*UP*UP*CP*GP*AP*CP*GP*AP*GP*AP*GP*AP*GP*AP*CP*C)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;4.8%(v/v) isopropanol, 0.096 M tacsimate, 1.92-1.95 M ammonium sulfate, and 10-11%(v/v) glycerol and then gradually exchanged into a cryo stabilizer solution containing 4.8%(v/v) isopropanol, 0.096 M tacsimate, 1.95 M ammonium sulfate and 19-27%(v/v) xylitol with CTP prior to freezing, VAPOR DIFFUSION, SITTING DROP, temperature 289K Resolution 2.69 Å R-free 0.256
2 Protein–RNA Monomer Protein × 1 RNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain E; UniProt 1749–2209 Fragment:unp residues 1749-2209 Mutation:L446D, C290A ;RNA (5'-R(P*GP*GP*GP*AP*GP*AP*UP*GP*AP*AP*AP*GP*UP*CP*UP*CP*CP*AP*GP*GP*UP*CP*UP*CP*UP*CP*UP*CP*GP*UP*CP*GP*AP*AP*A)-3') ; × 1 ;RNA (5'-R(*UP*GP*UP*UP*CP*GP*AP*CP*GP*AP*GP*AP*GP*AP*GP*AP*CP*C)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;4.8%(v/v) isopropanol, 0.096 M tacsimate, 1.92-1.95 M ammonium sulfate, and 10-11%(v/v) glycerol and then gradually exchanged into a cryo stabilizer solution containing 4.8%(v/v) isopropanol, 0.096 M tacsimate, 1.95 M ammonium sulfate and 19-27%(v/v) xylitol with CTP prior to freezing, VAPOR DIFFUSION, SITTING DROP, temperature 289K Resolution 2.69 Å R-free 0.256

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 249 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 Author chain E; 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 4k4w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4k4w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4k4w
Deposition date deposition_date2013-04-12
Structure title titlePoliovirus polymerase elongation complex (r5+2_form)
Keywords keywordspolymerase, RNA-dependent RNA polymerase, protein-RNA complex, Transferase-rna complex; Transferase/rna
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.35
Radius of gyration Rg (electron density) rg_electron46.39
Forward intensity I(0) i0299229000.00
Molecular weight molecular_weight128140.0 kDa
Excluded volume excluded_volume153830 ų
Envelope volume envelope_volume220940 ų
Hydration-shell volume shell_volume40356 ų
Envelope diameter envelope_diameter143.4
Shell Rg shell_rg50.15
Envelope Rg envelope_rg44.67
Shape Rg shape_rg46.44
Total Rg total_rg46.36
Total atoms total_atoms8920
Residues n_residues995
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 dmax134.4
Rg (real space) rg_real44.47
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real2.9420e+08
I(0) uncertainty (real space) i0_real_error4.0130e+06
Rg (reciprocal space) rg_reciprocal44.36
I(0) (reciprocal space) i0_reciprocal299100000.0000
Solution quality estimate total_estimate0.5357
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.6
Skewness Skewness skewness0.387
Kurtosis Kurtosis kurtosis-0.923
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha1.8320
Highest regularization parameter α highest_alpha73270000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.491; Stabil: 0.954; Sysdev: 0.000; Positv: 1.000; Valcen: 0.603; Smooth: 0.026

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4k4wa1
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_idd4k4wa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4k4we1
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_idd4k4we2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id4k4wA02
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_id4k4wA03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology960 — Mitochondrial Import Receptor Subunit Tom20; Chain A
Homologous superfamily homologous superfamily20
Domain ID domain_id4k4wE02
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_id4k4wE03
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)