7pq0

Crystal structure of the Burkholderia Lethal Factor 1 (BLF1) C94S inactive mutant in complex with human eIF4A - Crystal form B

Method: X-RAY DIFFRACTION Dmax: 87.2 Å Quality: REASONABLE

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

Burkholderia Lethal Factor 1 (BLF1)

Burkholderia pseudomallei (strain K96243)

UniProt Q63UP7

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–211 Mutation:C94S Eukaryotic initiation factor 4A-I × 1 (P60842) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290 K;0.1 M HEPES, 4 % (w/v) PEG 6000 Resolution 3.00 Å R-free 0.230

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q63UP7_BURPS
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–211; UniProt 1–211

Eukaryotic initiation factor 4A-I

Homo sapiens

UniProt P60842

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 20–406 Not recorded Burkholderia Lethal Factor 1 (BLF1) × 1 (Q63UP7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290 K;0.1 M HEPES, 4 % (w/v) PEG 6000 Resolution 3.00 Å R-free 0.230

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.

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

View Construct and Data Evidence
UniProt name IF4A1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 8–394; UniProt 20–406

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 7pq0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7pq0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7pq0
Deposition date deposition_date2021-09-15
Structure title titleCrystal structure of the Burkholderia Lethal Factor 1 (BLF1) C94S inactive mutant in complex with human eIF4A - Crystal form B
Keywords keywordsGlutamine deamidase toxin, cysteine protease, eIf4A complex, CNF1 family, TOXIN; TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.68
Radius of gyration Rg (electron density) rg_electron26.70
Forward intensity I(0) i074617000.00
Molecular weight molecular_weight67074.0 kDa
Excluded volume excluded_volume83783 ų
Envelope volume envelope_volume103840 ų
Hydration-shell volume shell_volume32319 ų
Envelope diameter envelope_diameter91.1
Shell Rg shell_rg34.13
Envelope Rg envelope_rg26.83
Shape Rg shape_rg26.68
Total Rg total_rg27.52
Total atoms total_atoms4716
Residues n_residues595
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 dmax87.2
Rg (real space) rg_real27.63
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real7.4620e+07
I(0) uncertainty (real space) i0_real_error1.0910e+06
Rg (reciprocal space) rg_reciprocal27.65
I(0) (reciprocal space) i0_reciprocal74620000.0000
Solution quality estimate total_estimate0.7125
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.6
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.466
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24660000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 0.177; Positv: 1.000; Valcen: 1.000; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7pq0B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id7pq0B02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)