4ibi

Ebola virus VP35 bound to small molecule

Method: X-RAY DIFFRACTION Dmax: 73.8 Å Quality: GOOD

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

Polymerase cofactor VP35

Ebola virus

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 215–340 Fragment:unp residues 215-340 1D8 3-{(2S)-2-(7-chloro-1,3-benzodioxol-5-yl)-4-hydroxy-5-oxo-3-[3-(trifluoromethyl)benzoyl]-2,5-dihydro-1H-pyrrol-1-yl}benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;100 mM sodium citrate, pH5.5, 15% PEG3350, 10%DMS, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.47 Å R-free 0.237
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 215–340 Fragment:unp residues 215-340 1D8 3-{(2S)-2-(7-chloro-1,3-benzodioxol-5-yl)-4-hydroxy-5-oxo-3-[3-(trifluoromethyl)benzoyl]-2,5-dihydro-1H-pyrrol-1-yl}benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;100 mM sodium citrate, pH5.5, 15% PEG3350, 10%DMS, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.47 Å R-free 0.237

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 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP35_EBOZM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–129; UniProt 215–340 Author chain B; PDBConstruct 4–129; UniProt 215–340

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 4ibi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4ibi
Deposition date deposition_date2012-12-08
Structure title titleEbola virus VP35 bound to small molecule
Keywords keywordsinterferon inhibitor domain, TRANSCRIPTION-TRANSCRIPTION inhibitor complex; TRANSCRIPTION/TRANSCRIPTION inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.71
Radius of gyration Rg (electron density) rg_electron20.66
Forward intensity I(0) i014404100.00
Molecular weight molecular_weight28676.0 kDa
Excluded volume excluded_volume36055 ų
Envelope volume envelope_volume43436 ų
Hydration-shell volume shell_volume18439 ų
Envelope diameter envelope_diameter78.2
Shell Rg shell_rg26.15
Envelope Rg envelope_rg20.89
Shape Rg shape_rg20.65
Total Rg total_rg21.53
Total atoms total_atoms2014
Residues n_residues250
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 dmax73.8
Rg (real space) rg_real21.80
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.4400e+07
I(0) uncertainty (real space) i0_real_error2.2360e+05
Rg (reciprocal space) rg_reciprocal21.78
I(0) (reciprocal space) i0_reciprocal14400000.0000
Solution quality estimate total_estimate0.7836
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.480
Kurtosis Kurtosis kurtosis-0.174
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2980000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.760; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.903; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4ibia_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.388 — Filoviridae VP35-like
Superfamily Superfamily superfamilyd.388.1 — Filoviridae VP35-like
Family Family familyd.388.1.1 — Filoviridae VP35
Domain ID domain_idd4ibib1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.388 — Filoviridae VP35-like
Superfamily Superfamily superfamilyd.388.1 — Filoviridae VP35-like
Family Family familyd.388.1.1 — Filoviridae VP35
Domain ID domain_idd4ibib2
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_id4ibiA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily950 — Filoviridae VP35, C-terminal inhibitory domain, helical subdomain
Domain ID domain_id4ibiA02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily70 — Filoviridae VP35, C-terminal inhibitory domain, beta-sheet subdomain
Domain ID domain_id4ibiB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily950 — Filoviridae VP35, C-terminal inhibitory domain, helical subdomain
Domain ID domain_id4ibiB02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily70 — Filoviridae VP35, C-terminal inhibitory domain, beta-sheet subdomain

8. Citations (1)

9. Files and Curves (10)