9yp2

Structure of HaCV P domain in complex with Nanobody 7

Method: X-RAY DIFFRACTION Dmax: 95.3 Å Quality: GOOD

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

Capsid protein

Hare calicivirus

UniProt A0A4D6I9J0

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1983–2321 Chain B; UniProt 1983–2321 Fragment:P domain Nanobody 7 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291.15 K;0.2 M Sodium fluoride, 20% PEG3350 Resolution 2.09 Å R-free 0.223

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A4D6I9J0_9CALI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–339; UniProt 1983–2321 Author chain B; PDBConstruct 1–339; UniProt 1983–2321

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 9yp2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yp2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yp2
Deposition date deposition_date2025-10-13
Structure title titleStructure of HaCV P domain in complex with Nanobody 7
Keywords keywordsNanobody, complex, 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_guinier29.25
Radius of gyration Rg (electron density) rg_electron28.24
Forward intensity I(0) i0135680000.00
Molecular weight molecular_weight91163.0 kDa
Excluded volume excluded_volume113440 ų
Envelope volume envelope_volume137720 ų
Hydration-shell volume shell_volume39943 ų
Envelope diameter envelope_diameter105.1
Shell Rg shell_rg36.03
Envelope Rg envelope_rg28.62
Shape Rg shape_rg28.20
Total Rg total_rg29.04
Total atoms total_atoms6441
Residues n_residues871
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 dmax95.3
Rg (real space) rg_real29.15
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.3570e+08
I(0) uncertainty (real space) i0_real_error2.1230e+06
Rg (reciprocal space) rg_reciprocal29.19
I(0) (reciprocal space) i0_reciprocal135700000.0000
Solution quality estimate total_estimate0.8906
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.1
Skewness Skewness skewness0.245
Kurtosis Kurtosis kurtosis-0.329
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42290000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)