9gvn

DEPEMOKIMAB FAB IN COMPLEX WITH INTERLEUKIN 5

Method: X-RAY DIFFRACTION Dmax: 131.7 Å Quality: GOOD

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

Interleukin-5

Homo sapiens

UniProt P05113

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 20–134 Chain B; UniProt 20–134 Not recorded Fab heavy chain × 2 Fab light chain × 2 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Morpheus EDO_P8K, Morpheus Carboxylic acids, Morpheus buffer system 2 Resolution 1.93 Å R-free 0.209

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–115; UniProt 20–134 Author chain B; PDBConstruct 1–115; UniProt 20–134

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 9gvn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9gvn
Deposition date deposition_date2024-09-25
最后修订 last_revision2026-01-14
Structure title titleDEPEMOKIMAB FAB IN COMPLEX WITH INTERLEUKIN 5
Keywords keywordsIL-5, ANTIBODY, COMPLEX, EPITOPE, CYTOKINE, GLYCOPROTEIN, IMMUNOGLOBULIN FOLD, 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_guinier41.42
Radius of gyration Rg (electron density) rg_electron41.25
Forward intensity I(0) i0217790000.00
Molecular weight molecular_weight120300.0 kDa
Excluded volume excluded_volume150560 ų
Envelope volume envelope_volume209830 ų
Hydration-shell volume shell_volume42650 ų
Envelope diameter envelope_diameter133.5
Shell Rg shell_rg46.15
Envelope Rg envelope_rg40.77
Shape Rg shape_rg41.21
Total Rg total_rg41.61
Total atoms total_atoms8460
Residues n_residues1092
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 dmax131.7
Rg (real space) rg_real41.51
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real2.1780e+08
I(0) uncertainty (real space) i0_real_error3.7580e+06
Rg (reciprocal space) rg_reciprocal41.43
I(0) (reciprocal space) i0_reciprocal217800000.0000
Solution quality estimate total_estimate0.8265
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.1
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.778
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16320000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.938; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)