9ip3

Cryo-EM structure of the RNA-dependent RNA polymerase complex in a compact conformation from Ebola virus

Method: ELECTRON MICROSCOPY Dmax: 113.4 Å Quality: REASONABLE

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

Maltose/maltodextrin-binding periplasmic protein,RNA-directed RNA polymerase L

Ebola virus - Eckron (Zaire, 1976)

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 29–392 Chain B; UniProt 29–392 Chain C; UniProt 29–392 Chain D; UniProt 29–392 Chain E; UniProt 29–392 Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES, 300 mM NaCl, 1 mM TCEP, 6 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 47–410; UniProt 29–392 Author chain B; PDBConstruct 15–378; UniProt 29–392 Author chain C; PDBConstruct 15–378; UniProt 29–392 Author chain D; PDBConstruct 15–378; UniProt 29–392 Author chain E; PDBConstruct 15–378; UniProt 29–392

Maltose/maltodextrin-binding periplasmic protein,RNA-directed RNA polymerase L

Ebola virus - Eckron (Zaire, 1976)

UniProt Q05318

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–1400 Not recorded Maltose/maltodextrin-binding periplasmic protein,Polymerase cofactor VP35 × 4 (P0AEX9,Q05127) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES, 300 mM NaCl, 1 mM TCEP, 6 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name L_EBOZM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 430–1829; UniProt 1–1400

Maltose/maltodextrin-binding periplasmic protein,Polymerase cofactor VP35

Ebola virus - Eckron (Zaire, 1976)

UniProt Q05127

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 80–340 Chain C; UniProt 80–340 Chain D; UniProt 80–340 Chain E; UniProt 80–340 Not recorded Maltose/maltodextrin-binding periplasmic protein,RNA-directed RNA polymerase L × 1 (P0AEX9,Q05318) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES, 300 mM NaCl, 1 mM TCEP, 6 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

25 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP35_EBOZM
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 397–657; UniProt 80–340 Author chain C; PDBConstruct 397–657; UniProt 80–340 Author chain D; PDBConstruct 397–657; UniProt 80–340 Author chain E; PDBConstruct 397–657; UniProt 80–340

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 9ip3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ip3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ip3
Deposition date deposition_date2024-07-10
Structure title titleCryo-EM structure of the RNA-dependent RNA polymerase complex in a compact conformation from Ebola virus
Keywords keywordsRNA-dependent RNA polymerase complex, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.98
Radius of gyration Rg (electron density) rg_electron36.15
Forward intensity I(0) i0533135000.00
Molecular weight molecular_weight191290.0 kDa
Excluded volume excluded_volume240950 ų
Envelope volume envelope_volume302660 ų
Hydration-shell volume shell_volume67006 ų
Envelope diameter envelope_diameter120.0
Shell Rg shell_rg44.40
Envelope Rg envelope_rg35.82
Shape Rg shape_rg36.12
Total Rg total_rg36.79
Total atoms total_atoms13457
Residues n_residues1693
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 dmax113.4
Rg (real space) rg_real36.73
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real5.3310e+08
I(0) uncertainty (real space) i0_real_error7.6150e+06
Rg (reciprocal space) rg_reciprocal36.89
I(0) (reciprocal space) i0_reciprocal533200000.0000
Solution quality estimate total_estimate0.6701
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.1
Skewness Skewness skewness0.124
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha107600000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 0.048; Positv: 1.000; Valcen: 0.978; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)