3di2

Crystal structure of the complex of human interleukin-7 with unglycosylated human interleukin-7 receptor alpha ectodomain

Method: X-RAY DIFFRACTION Dmax: 133.7 Å Quality: GOOD

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

Interleukin-7

Homo sapiens

UniProt P13232

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 26–177 Fragment:UNP residues 26 to 177 Mutation:E106A Interleukin-7 receptor subunit alpha × 1 (P16871) 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;20% w/v PEG 8000, 0.1M MES, 0.2 M calcium acetate, pH 6.0, sitting drop, temperature 292K Resolution 2.70 Å R-free 0.267
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 26–177 Fragment:UNP residues 26 to 177 Mutation:E106A Interleukin-7 receptor subunit alpha × 1 (P16871) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;20% w/v PEG 8000, 0.1M MES, 0.2 M calcium acetate, pH 6.0, sitting drop, temperature 292K Resolution 2.70 Å R-free 0.267

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–154; UniProt 26–177 Author chain C; PDBConstruct 3–154; UniProt 26–177

Interleukin-7 receptor subunit alpha

Homo sapiens

UniProt P16871

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 B; UniProt 21–239 Fragment:UNP residues 21 to 239 (ligand binding ectodomain) Mutation:I118V Interleukin-7 × 1 (P13232) 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;20% w/v PEG 8000, 0.1M MES, 0.2 M calcium acetate, pH 6.0, sitting drop, temperature 292K Resolution 2.70 Å R-free 0.267
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 21–239 Fragment:UNP residues 21 to 239 (ligand binding ectodomain) Mutation:I118V Interleukin-7 × 1 (P13232) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;20% w/v PEG 8000, 0.1M MES, 0.2 M calcium acetate, pH 6.0, sitting drop, temperature 292K Resolution 2.70 Å R-free 0.267

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.

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

View Construct and Data Evidence
UniProt name IL7RA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–223; UniProt 21–239 Author chain D; PDBConstruct 5–223; UniProt 21–239

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 3di2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3di2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3di2
Deposition date deposition_date2008-06-19
Structure title titleCrystal structure of the complex of human interleukin-7 with unglycosylated human interleukin-7 receptor alpha ectodomain
Keywords keywords;interleukin, cytokine, cytokine receptor, ectodomain, Glycoprotein, Growth factor, Secreted, Alternative splicing, Disease mutation, Membrane, Phosphoprotein, Polymorphism, Receptor, SCID, Transmembrane, 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_guinier43.78
Radius of gyration Rg (electron density) rg_electron43.65
Forward intensity I(0) i065606400.00
Molecular weight molecular_weight67931.0 kDa
Excluded volume excluded_volume85709 ų
Envelope volume envelope_volume135180 ų
Hydration-shell volume shell_volume26770 ų
Envelope diameter envelope_diameter140.4
Shell Rg shell_rg47.44
Envelope Rg envelope_rg41.30
Shape Rg shape_rg43.61
Total Rg total_rg43.99
Total atoms total_atoms4790
Residues n_residues616
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 dmax133.7
Rg (real space) rg_real44.03
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real6.5610e+07
I(0) uncertainty (real space) i0_real_error1.1850e+06
Rg (reciprocal space) rg_reciprocal43.78
I(0) (reciprocal space) i0_reciprocal65590000.0000
Solution quality estimate total_estimate0.7654
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.0
Skewness Skewness skewness0.199
Kurtosis Kurtosis kurtosis-0.896
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2168000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.624; Smooth: 0.133

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id3di2A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily50
Domain ID domain_id3di2B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1870
Domain ID domain_id3di2B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3di2C00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily50
Domain ID domain_id3di2D01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1870
Domain ID domain_id3di2D02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)