4nzd

Interleukin 21 receptor

Method: X-RAY DIFFRACTION Dmax: 128.2 Å Quality: REASONABLE

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

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 20–232 Not recorded ;alpha-D-mannopyranose-(1-6)-beta-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 MAN alpha-D-mannopyranose × 1 NA SODIUM ION × 3 CL CHLORIDE ION × 4 TLA L(+)-TARTARIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;278 K;5 mg/ml Protein in 10 mM Hepes, 150 mM NaCl, pH7.5 Crystalized in 1M Potassium sodium tartrate tetrahydrate, 3% W/V Peg5000 and 0.1 M tris Ph 8.5. Drops were 1:1, VAPOR DIFFUSION, SITTING DROP, temperature 278K Resolution 2.75 Å R-free 0.275
2 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 20–232 Not recorded ;alpha-D-mannopyranose-(1-6)-beta-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 MAN alpha-D-mannopyranose × 1 CL CHLORIDE ION × 5 TLA L(+)-TARTARIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;278 K;5 mg/ml Protein in 10 mM Hepes, 150 mM NaCl, pH7.5 Crystalized in 1M Potassium sodium tartrate tetrahydrate, 3% W/V Peg5000 and 0.1 M tris Ph 8.5. Drops were 1:1, VAPOR DIFFUSION, SITTING DROP, temperature 278K Resolution 2.75 Å R-free 0.275
3 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 20–232 Not recorded ;alpha-D-mannopyranose-(1-6)-beta-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 MAN alpha-D-mannopyranose × 1 NA SODIUM ION × 2 CL CHLORIDE ION × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;278 K;5 mg/ml Protein in 10 mM Hepes, 150 mM NaCl, pH7.5 Crystalized in 1M Potassium sodium tartrate tetrahydrate, 3% W/V Peg5000 and 0.1 M tris Ph 8.5. Drops were 1:1, VAPOR DIFFUSION, SITTING DROP, temperature 278K Resolution 2.75 Å R-free 0.275
4 Other combination Homooligomer Protein × 6 其他Polymer 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 20–232 Chain B; UniProt 20–232 Chain C; UniProt 20–232 Not recorded ;alpha-D-mannopyranose-(1-6)-beta-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 ; × 6 MAN alpha-D-mannopyranose × 6 NA SODIUM ION × 10 CL CHLORIDE ION × 22 TLA L(+)-TARTARIC ACID × 6 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;278 K;5 mg/ml Protein in 10 mM Hepes, 150 mM NaCl, pH7.5 Crystalized in 1M Potassium sodium tartrate tetrahydrate, 3% W/V Peg5000 and 0.1 M tris Ph 8.5. Drops were 1:1, VAPOR DIFFUSION, SITTING DROP, temperature 278K Resolution 2.75 Å R-free 0.275

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–213; UniProt 20–232 Author chain B; PDBConstruct 1–213; UniProt 20–232 Author chain C; PDBConstruct 1–213; UniProt 20–232

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 4nzd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4nzd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4nzd
Deposition date deposition_date2013-12-12
Structure title titleInterleukin 21 receptor
Keywords keywordsFibronectine III domain, Interleukin 21, Glycosylated, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.53
Radius of gyration Rg (electron density) rg_electron33.01
Forward intensity I(0) i098345300.00
Molecular weight molecular_weight76035.0 kDa
Excluded volume excluded_volume93946 ų
Envelope volume envelope_volume142840 ų
Hydration-shell volume shell_volume37268 ų
Envelope diameter envelope_diameter135.0
Shell Rg shell_rg37.81
Envelope Rg envelope_rg33.69
Shape Rg shape_rg33.02
Total Rg total_rg33.41
Total atoms total_atoms5332
Residues n_residues628
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 dmax128.2
Rg (real space) rg_real33.56
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real9.8350e+07
I(0) uncertainty (real space) i0_real_error1.6700e+06
Rg (reciprocal space) rg_reciprocal33.54
I(0) (reciprocal space) i0_reciprocal98340000.0000
Solution quality estimate total_estimate0.7487
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.9
Skewness Skewness skewness0.372
Kurtosis Kurtosis kurtosis-0.185
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17400000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.648; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.784; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4nzdA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4nzdB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4nzdB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4nzdC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)