9ezi

Structure of single-domain antibody VHH_h5 in complex with human Vsig4

Method: X-RAY DIFFRACTION Dmax: 71.5 Å Quality: GOOD

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

V-set and immunoglobulin domain-containing protein 4

Homo sapiens

UniProt Q9Y279

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 20–137 Not recorded VHH_h5 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0,1M Bis-Tris pH 6.5 and 30% PEG3350 Resolution 1.97 Å R-free 0.243

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.

11 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VSIG4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–118; UniProt 20–137

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 9ezi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ezi
Deposition date deposition_date2024-04-12
Structure title titleStructure of single-domain antibody VHH_h5 in complex with human Vsig4
Keywords keywordsNanobody, Mutations, CDR2, CDR3, hVsig4, B7 family, immune regulatory proteins, 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_guinier20.22
Radius of gyration Rg (electron density) rg_electron19.53
Forward intensity I(0) i013255600.00
Molecular weight molecular_weight26659.0 kDa
Excluded volume excluded_volume33018 ų
Envelope volume envelope_volume38356 ų
Hydration-shell volume shell_volume17156 ų
Envelope diameter envelope_diameter73.2
Shell Rg shell_rg25.05
Envelope Rg envelope_rg19.86
Shape Rg shape_rg19.48
Total Rg total_rg20.43
Total atoms total_atoms1881
Residues n_residues239
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 dmax71.5
Rg (real space) rg_real20.25
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real1.3260e+07
I(0) uncertainty (real space) i0_real_error1.9780e+05
Rg (reciprocal space) rg_reciprocal20.25
I(0) (reciprocal space) i0_reciprocal13260000.0000
Solution quality estimate total_estimate0.8548
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.410
Kurtosis Kurtosis kurtosis-0.287
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4451000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.736; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.917; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)