3v44

Crystal structure of the N-terminal fragment of zebrafish TLR5

Method: X-RAY DIFFRACTION Dmax: 106.1 Å Quality: GOOD

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

Toll-like receptor 5b and variable lymphocyte receptor B.61 chimeric protein

Eptatretus burgeri

UniProt B3DIN1

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 22–342 Fragment:zebrafish Toll-like receptor 5b (UNP residues 22-342) and hagfish variable lymphocyte receptor B.61 (UNP residues 126-200) Mutation:V24E, L124V, Q159K, R227K, S229T, D334N NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;20% MPD, 0.1 M Hepes pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.83 Å R-free 0.238

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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B3DIN1_DANRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–325; UniProt 22–342

Toll-like receptor 5b and variable lymphocyte receptor B.61 chimeric protein

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 126–200 Fragment:zebrafish Toll-like receptor 5b (UNP residues 22-342) and hagfish variable lymphocyte receptor B.61 (UNP residues 126-200) Mutation:V24E, L124V, Q159K, R227K, S229T, D334N NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;20% MPD, 0.1 M Hepes pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.83 Å R-free 0.238

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 50 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 326–400; 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 3v44

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3v44
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3v44
Deposition date deposition_date2011-12-14
Structure title titleCrystal structure of the N-terminal fragment of zebrafish TLR5
Keywords keywordsflagellin, innate immunity, Leucine-rich repeat, innate immune receptor, 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_guinier27.54
Radius of gyration Rg (electron density) rg_electron26.80
Forward intensity I(0) i033134400.00
Molecular weight molecular_weight45289.0 kDa
Excluded volume excluded_volume56964 ų
Envelope volume envelope_volume71163 ų
Hydration-shell volume shell_volume23220 ų
Envelope diameter envelope_diameter109.7
Shell Rg shell_rg32.40
Envelope Rg envelope_rg27.50
Shape Rg shape_rg26.77
Total Rg total_rg27.53
Total atoms total_atoms3188
Residues n_residues401
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 dmax106.1
Rg (real space) rg_real27.80
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real3.3130e+07
I(0) uncertainty (real space) i0_real_error5.8790e+05
Rg (reciprocal space) rg_reciprocal27.72
I(0) (reciprocal space) i0_reciprocal33130000.0000
Solution quality estimate total_estimate0.7517
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.523
Kurtosis Kurtosis kurtosis-0.183
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9435000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.433; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.477; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)