9tq6

Antibody-antigen complex

Method: X-RAY DIFFRACTION Dmax: 108.5 Å Quality: GOOD

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

Beta-nerve growth factor

OrganismNot specified

UniProt P01138

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Q; UniProt 169–178 Non-standard monomer:Yes (specific site not provided by mmCIF) Antibody Fab fragment heavy chain × 1 Antibody Fab fragment light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;50 mM imidazole, pH 7, 18% PEG 3350 Resolution 2.40 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain P; UniProt 169–178 Non-standard monomer:Yes (specific site not provided by mmCIF) Antibody Fab fragment heavy chain × 1 Antibody Fab fragment light chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;50 mM imidazole, pH 7, 18% PEG 3350 Resolution 2.40 Å R-free 0.276

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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NGF_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 2–11; UniProt 169–178 Author chain Q; PDBConstruct 2–11; UniProt 169–178

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 9tq6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9tq6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9tq6
Deposition date deposition_date2025-12-19
最后修订 last_revision2026-05-27
Structure title titleAntibody-antigen complex
Keywords keywordsantibody, nitrotyrosine, complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.63
Radius of gyration Rg (electron density) rg_electron32.84
Forward intensity I(0) i0145307000.00
Molecular weight molecular_weight95353.0 kDa
Excluded volume excluded_volume118940 ų
Envelope volume envelope_volume161210 ų
Hydration-shell volume shell_volume41368 ų
Envelope diameter envelope_diameter108.6
Shell Rg shell_rg39.40
Envelope Rg envelope_rg32.03
Shape Rg shape_rg32.83
Total Rg total_rg33.45
Total atoms total_atoms6719
Residues n_residues866
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 dmax108.5
Rg (real space) rg_real33.56
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real1.4530e+08
I(0) uncertainty (real space) i0_real_error2.6110e+06
Rg (reciprocal space) rg_reciprocal33.61
I(0) (reciprocal space) i0_reciprocal145300000.0000
Solution quality estimate total_estimate0.8993
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.9
Skewness Skewness skewness0.215
Kurtosis Kurtosis kurtosis-0.460
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13540000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)