8ent

Interleukin-21 signaling complex with IL-21R and IL-2Rg

Method: X-RAY DIFFRACTION Dmax: 198.5 Å Quality: GOOD

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

Interleukin-21

Homo sapiens

UniProt Q9HBE4

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 × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 30–162 Mutation:N68Q Interleukin-21 receptor × 1 (Q9HBE5) Cytokine receptor common subunit gamma × 1 (P31785) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 30–162 Mutation:N68Q Interleukin-21 receptor × 1 (Q9HBE5) Cytokine receptor common subunit gamma × 1 (P31785) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300
3 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 30–162 Mutation:N68Q Interleukin-21 receptor × 1 (Q9HBE5) Cytokine receptor common subunit gamma × 1 (P31785) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300
4 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain J; UniProt 30–162 Mutation:N68Q Interleukin-21 receptor × 1 (Q9HBE5) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 EDO 1,2-ETHANEDIOL × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300

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.

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

View Construct and Data Evidence
UniProt name IL21_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–133; UniProt 30–162 Author chain D; PDBConstruct 1–133; UniProt 30–162 Author chain G; PDBConstruct 1–133; UniProt 30–162 Author chain J; PDBConstruct 1–133; UniProt 30–162

Interleukin-21 receptor

Homo sapiens

UniProt Q9HBE5

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 × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 20–229 Mutation:N78Q, N85Q, N106D, N116Q Interleukin-21 × 1 (Q9HBE4) Cytokine receptor common subunit gamma × 1 (P31785) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 20–229 Mutation:N78Q, N85Q, N106D, N116Q Interleukin-21 × 1 (Q9HBE4) Cytokine receptor common subunit gamma × 1 (P31785) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300
3 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 20–229 Mutation:N78Q, N85Q, N106D, N116Q Interleukin-21 × 1 (Q9HBE4) Cytokine receptor common subunit gamma × 1 (P31785) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300
4 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain K; UniProt 20–229 Mutation:N78Q, N85Q, N106D, N116Q Interleukin-21 × 1 (Q9HBE4) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 EDO 1,2-ETHANEDIOL × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300

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.

5 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL21R_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–210; UniProt 20–229 Author chain E; PDBConstruct 1–210; UniProt 20–229 Author chain H; PDBConstruct 1–210; UniProt 20–229 Author chain K; PDBConstruct 1–210; UniProt 20–229

Cytokine receptor common subunit gamma

Homo sapiens

UniProt P31785

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 × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 55–254 Mutation:N53Q Interleukin-21 × 1 (Q9HBE4) Interleukin-21 receptor × 1 (Q9HBE5) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 55–254 Mutation:N53Q Interleukin-21 × 1 (Q9HBE4) Interleukin-21 receptor × 1 (Q9HBE5) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300
3 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 55–254 Mutation:N53Q Interleukin-21 × 1 (Q9HBE4) Interleukin-21 receptor × 1 (Q9HBE5) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;0.1M Tris pH 8, 20% PEG 6000 Resolution 2.83 Å R-free 0.300

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.

13 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL2RG_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–201; UniProt 55–254 Author chain F; PDBConstruct 2–201; UniProt 55–254 Author chain I; PDBConstruct 2–201; UniProt 55–254

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 8ent

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ent
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ent
Deposition date deposition_date2022-09-30
Structure title titleInterleukin-21 signaling complex with IL-21R and IL-2Rg
Keywords keywordsIL-21, receptor, complex, signaling, CYTOKINE, CYTOKINE-CYTOKINE RECEPTOR complex; CYTOKINE/CYTOKINE RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier55.58
Radius of gyration Rg (electron density) rg_electron55.88
Forward intensity I(0) i0744706000.00
Molecular weight molecular_weight224140.0 kDa
Excluded volume excluded_volume278700 ų
Envelope volume envelope_volume436790 ų
Hydration-shell volume shell_volume67715 ų
Envelope diameter envelope_diameter211.7
Shell Rg shell_rg56.38
Envelope Rg envelope_rg54.14
Shape Rg shape_rg55.82
Total Rg total_rg56.09
Total atoms total_atoms15780
Residues n_residues1888
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 dmax198.5
Rg (real space) rg_real55.87
Rg uncertainty (real space) rg_real_error2.78
I(0) (real space) i0_real7.4470e+08
I(0) uncertainty (real space) i0_real_error1.6380e+07
Rg (reciprocal space) rg_reciprocal55.33
I(0) (reciprocal space) i0_reciprocal744100000.0000
Solution quality estimate total_estimate0.8531
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.9
Skewness Skewness skewness0.429
Kurtosis Kurtosis kurtosis-0.202
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha32080000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.769

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)