4gh9

Crystal structure of Marburg virus VP35 RNA binding domain

Method: X-RAY DIFFRACTION Dmax: 51.1 Å Quality: GOOD

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

Polymerase cofactor VP35

Marburg virus

UniProt P35259

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 204–329 Fragment:UNP residues 204-329 ACT ACETATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;298 K;2-2.4 M ammonium sulphate, 100 mM sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.65 Å R-free 0.217

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP35_MABVM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–146; UniProt 204–329

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 4gh9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gh9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gh9
Deposition date deposition_date2012-08-07
Structure title titleCrystal structure of Marburg virus VP35 RNA binding domain
Keywords keywordsViral polymerase, Interferon inhibition, double stranded viral RNA, VIRAL PROTEIN, RNA BINDING PROTEIN; VIRAL PROTEIN,RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.87
Radius of gyration Rg (electron density) rg_electron14.37
Forward intensity I(0) i03532930.00
Molecular weight molecular_weight13704.0 kDa
Excluded volume excluded_volume17396 ų
Envelope volume envelope_volume19456 ų
Hydration-shell volume shell_volume11740 ų
Envelope diameter envelope_diameter50.9
Shell Rg shell_rg19.75
Envelope Rg envelope_rg14.70
Shape Rg shape_rg14.36
Total Rg total_rg15.57
Total atoms total_atoms967
Residues n_residues122
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 dmax51.1
Rg (real space) rg_real15.81
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real3.5330e+06
I(0) uncertainty (real space) i0_real_error4.3510e+04
Rg (reciprocal space) rg_reciprocal15.82
I(0) (reciprocal space) i0_reciprocal3533000.0000
Solution quality estimate total_estimate0.8110
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.1
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha548700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4gh9a_
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

CATH v4.4 (2 domains)

Domain ID domain_id4gh9A01
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_id4gh9A02
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)