11ha

Crystal structure of a GII.4 norovirus capsid P domain in complex with neutralizing antibody 24C10

Method: X-RAY DIFFRACTION Dmax: 138.2 Å Quality: GOOD

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

Major capsid protein VP1

Norovirus GII.4 Sydney 2012

UniProt A0A1P8DD09

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 221–530 Chain B; UniProt 221–530 Not recorded 24C10 Light Chain × 2 24C10 Heavy Chain × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;297.15 K;0.2 M HEPES: NaOH, pH 7.5, 8 % (w/v) PEG 8000, 8 % (v/v) Ethylene Glycol Resolution 2.70 Å R-free 0.245

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 A0A1P8DD09_NORV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–311; UniProt 221–530 Author chain B; PDBConstruct 2–311; UniProt 221–530

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 11ha

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 11ha
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2. Structure Basics 2. Structure Basics

Entry ID entry_id11ha
Deposition date deposition_date2026-02-23
最后修订 last_revision2026-05-27
Structure title titleCrystal structure of a GII.4 norovirus capsid P domain in complex with neutralizing antibody 24C10
Keywords keywordsNorovirus GII.4, P domain, Capsid protein, Antibody, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.21
Radius of gyration Rg (electron density) rg_electron42.41
Forward intensity I(0) i0387045000.00
Molecular weight molecular_weight158630.0 kDa
Excluded volume excluded_volume197130 ų
Envelope volume envelope_volume259840 ų
Hydration-shell volume shell_volume53623 ų
Envelope diameter envelope_diameter140.9
Shell Rg shell_rg44.58
Envelope Rg envelope_rg42.76
Shape Rg shape_rg42.36
Total Rg total_rg42.66
Total atoms total_atoms11177
Residues n_residues1451
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 dmax138.2
Rg (real space) rg_real42.36
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real3.8700e+08
I(0) uncertainty (real space) i0_real_error6.5600e+06
Rg (reciprocal space) rg_reciprocal42.21
I(0) (reciprocal space) i0_reciprocal387000000.0000
Solution quality estimate total_estimate0.8140
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.4
Skewness Skewness skewness0.370
Kurtosis Kurtosis kurtosis-0.613
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50490000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.946; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)