6bxc

Crystal structure of N-terminal fragment of Zebrafish Toll-Like Receptor 5 (TLR5) with Lamprey Variable Lymphocyte Receptor 9 (VLR9) bound

Method: X-RAY DIFFRACTION Dmax: 120.5 Å Quality: REASONABLE

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

Toll-like receptor 5b, Variable lymphocyte receptor B chimera

Eptatretus burgeri

UniProt F8W3J5

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 28–396 Not recorded Variable Lymphocyte Receptor 9 (VLR9) × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;15% Peg3350, 170 mM MgNO3, 80 mM MES pH 6.0, 15% ethylene glycol Resolution 2.50 Å R-free 0.270
2 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 28–396 Not recorded Variable Lymphocyte Receptor 9 (VLR9) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;15% Peg3350, 170 mM MgNO3, 80 mM MES pH 6.0, 15% ethylene glycol Resolution 2.50 Å R-free 0.270

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F8W3J5_DANRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–373; UniProt 28–396 Author chain B; PDBConstruct 5–373; UniProt 28–396

Toll-like receptor 5b, Variable lymphocyte receptor B chimera

Eptatretus burgeri

UniProt Q4G1L2

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 126–200 Not recorded Variable Lymphocyte Receptor 9 (VLR9) × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;15% Peg3350, 170 mM MgNO3, 80 mM MES pH 6.0, 15% ethylene glycol Resolution 2.50 Å R-free 0.270
2 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 126–200 Not recorded Variable Lymphocyte Receptor 9 (VLR9) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;15% Peg3350, 170 mM MgNO3, 80 mM MES pH 6.0, 15% ethylene glycol Resolution 2.50 Å R-free 0.270

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.

30 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q4G1L2_EPTBU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 374–448; UniProt 126–200 Author chain B; PDBConstruct 374–448; UniProt 126–200

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 6bxc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6bxc
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6bxc
Deposition date deposition_date2017-12-18
Structure title titleCrystal structure of N-terminal fragment of Zebrafish Toll-Like Receptor 5 (TLR5) with Lamprey Variable Lymphocyte Receptor 9 (VLR9) bound
Keywords keywordsVLR, LEUCINE-RICH REPEAT, antibody, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.49
Radius of gyration Rg (electron density) rg_electron35.76
Forward intensity I(0) i0265825000.00
Molecular weight molecular_weight133480.0 kDa
Excluded volume excluded_volume167800 ų
Envelope volume envelope_volume217600 ų
Hydration-shell volume shell_volume50838 ų
Envelope diameter envelope_diameter127.2
Shell Rg shell_rg42.10
Envelope Rg envelope_rg35.49
Shape Rg shape_rg35.75
Total Rg total_rg36.26
Total atoms total_atoms9394
Residues n_residues1213
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 dmax120.5
Rg (real space) rg_real36.44
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real2.6580e+08
I(0) uncertainty (real space) i0_real_error4.0720e+06
Rg (reciprocal space) rg_reciprocal36.47
I(0) (reciprocal space) i0_reciprocal265800000.0000
Solution quality estimate total_estimate0.6872
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.7
Skewness Skewness skewness0.308
Kurtosis Kurtosis kurtosis-0.279
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53560000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 0.159; Positv: 1.000; Valcen: 0.995; Smooth: 0.869

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)