2z62

Crystal structure of the TV3 hybrid of human TLR4 and hagfish VLRB.61

Method: X-RAY DIFFRACTION Dmax: 80.0 Å Quality: GOOD

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

Toll-like receptor 4, Variable lymphocyte receptor B

Eptatretus burgeri

UniProt O00206

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 其他Polymer 3 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–228 Fragment:TLR4, UNP residues 27-228(human), VLRB.61, UNP residues 128-199(Inshore hagfish) ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;296 K;0.2M NaCl, 0.1M Bis-Tris Propane, 33% PEG 1000, pH 5.50, VAPOR DIFFUSION, temperature 296K Resolution 1.70 Å R-free 0.208

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.

14 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TLR4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–202; UniProt 27–228

Toll-like receptor 4, Variable lymphocyte receptor B

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 其他Polymer 3 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 128–199 Fragment:TLR4, UNP residues 27-228(human), VLRB.61, UNP residues 128-199(Inshore hagfish) ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;296 K;0.2M NaCl, 0.1M Bis-Tris Propane, 33% PEG 1000, pH 5.50, VAPOR DIFFUSION, temperature 296K Resolution 1.70 Å R-free 0.208

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 205–276; UniProt 128–199

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 2z62

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2z62
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2z62
Deposition date deposition_date2007-07-22
Structure title titleCrystal structure of the TV3 hybrid of human TLR4 and hagfish VLRB.61
Keywords keywords;TLR, Toll-like receptor, VLR hybrid, MD-2, LPS, Glycoprotein, Immune response, Inflammatory response, Innate immunity, Leucine-rich repeat, Membrane, Transmembrane, 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_guinier23.01
Radius of gyration Rg (electron density) rg_electron22.04
Forward intensity I(0) i017877800.00
Molecular weight molecular_weight32792.0 kDa
Excluded volume excluded_volume41385 ų
Envelope volume envelope_volume48749 ų
Hydration-shell volume shell_volume19460 ų
Envelope diameter envelope_diameter84.1
Shell Rg shell_rg27.79
Envelope Rg envelope_rg22.23
Shape Rg shape_rg22.00
Total Rg total_rg22.93
Total atoms total_atoms2304
Residues n_residues276
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 dmax80.0
Rg (real space) rg_real23.10
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real1.7880e+07
I(0) uncertainty (real space) i0_real_error2.6080e+05
Rg (reciprocal space) rg_reciprocal23.08
I(0) (reciprocal space) i0_reciprocal17880000.0000
Solution quality estimate total_estimate0.8489
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.440
Kurtosis Kurtosis kurtosis-0.323
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2467000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.734; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.892; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2z62A00
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor

8. Citations (1)

9. Files and Curves (10)