9rag

Influenza A/H7N9 polymerase in complex with a 70-mer RNA template, in stalled elongation.

Method: ELECTRON MICROSCOPY Dmax: 123.8 Å Quality: GOOD

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

Polymerase acidic protein

Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))

UniProt M9TI86

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–716 Mutation:E349K; R490I Polymerase basic protein 2 × 1 (A0A024E1J5) RNA Pol II CTD 6 repeats (site 1A/2A) × 1 RNA product × 1 RNA-directed RNA polymerase catalytic subunit × 1 (S5ME50) RNA template (70-mer) × 1 MG MAGNESIUM ION × 3 POP PYROPHOSPHATE 2- × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 1.99 Å

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.

21 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name M9TI86_9INFA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–716; UniProt 1–716

Polymerase basic protein 2

Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))

UniProt A0A024E1J5

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 1–759 Mutation:G74R; K627; D701 Polymerase acidic protein × 1 (M9TI86) RNA Pol II CTD 6 repeats (site 1A/2A) × 1 RNA product × 1 RNA-directed RNA polymerase catalytic subunit × 1 (S5ME50) RNA template (70-mer) × 1 MG MAGNESIUM ION × 3 POP PYROPHOSPHATE 2- × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 1.99 Å

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A024E1J5_9INFA
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–759; UniProt 1–759

RNA-directed RNA polymerase catalytic subunit

Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))

UniProt S5ME50

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 1–757 Mutation:K577G Polymerase acidic protein × 1 (M9TI86) Polymerase basic protein 2 × 1 (A0A024E1J5) RNA Pol II CTD 6 repeats (site 1A/2A) × 1 RNA product × 1 RNA template (70-mer) × 1 MG MAGNESIUM ION × 3 POP PYROPHOSPHATE 2- × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 1.99 Å

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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S5ME50_9INFA
Isoform
PDB entities 5
Chains and sequence ranges Author chain B; PDBConstruct 1–757; UniProt 1–757

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 9rag

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rag
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rag
Deposition date deposition_date2025-05-20
Structure title titleInfluenza A/H7N9 polymerase in complex with a 70-mer RNA template, in stalled elongation.
Keywords keywordsInfluenza polymerase, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.21
Radius of gyration Rg (electron density) rg_electron37.14
Forward intensity I(0) i0758461000.00
Molecular weight molecular_weight211800.0 kDa
Excluded volume excluded_volume259600 ų
Envelope volume envelope_volume326280 ų
Hydration-shell volume shell_volume69990 ų
Envelope diameter envelope_diameter133.4
Shell Rg shell_rg45.33
Envelope Rg envelope_rg37.09
Shape Rg shape_rg37.17
Total Rg total_rg37.45
Total atoms total_atoms29018
Residues n_residues1756
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 dmax123.8
Rg (real space) rg_real37.10
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real7.5850e+08
I(0) uncertainty (real space) i0_real_error1.2350e+07
Rg (reciprocal space) rg_reciprocal37.17
I(0) (reciprocal space) i0_reciprocal758500000.0000
Solution quality estimate total_estimate0.8724
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.2
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.193
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha218400000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)