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5uwc

Cytokine-receptor complex

Method: X-RAY DIFFRACTION Dmax: 87.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Interleukin-3 receptor subunit alpha

Homo sapiens

UniProt P26951

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 × 2 其他Polymer 1 PDB declaration: dimeric（2） Consistent with protein copy count Chain G； UniProt 20–307 Fragment：UNP residues 20-307 Mutation：N212Q, A298V Interleukin-3 × 1 （P08700） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CIT CITRIC ACID × 2 IMD IMIDAZOLE × 1 EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；20% PEG 8000, 200 mM NaCl and 100 mM citrate-phosphate buffer pH 4.8 Resolution 2.40 Å R-free 0.242

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.

Other PDB Difference from Current Entry 5UWC Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4JZJ Crystal Structure of Receptor-Fab Complex Deposited 2013-04-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric
Chain C 20–307（288 aa） Fragment：DOMAIN 2, DOMAIN 3, UNP residues 20-307
Chain D 20–307（288 aa） Fragment：DOMAIN 2, DOMAIN 3, UNP residues 20-307
Mutation：Deletion R145, A298V Mutation：Deletion R145, A298V NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；293 K；22% PEG 3350, 200mM Sodium Malonate, 100mM Citrate Buffer, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.80 Å R-free 0.244
5UV8 Interleukin-3 Receptor Complex Deposited 2017-02-19 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 20–307（288 aa） Fragment：UNP residues 20-307
Mutation：N212Q, A298V NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 8000, 200 mM NaCI, 100 mM citrate-phosphate buffer pH 5
Resolution 2.70 Å R-free 0.286
5UV8 Interleukin-3 Receptor Complex Deposited 2017-02-19 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 20–307（288 aa） Fragment：UNP residues 20-307
Mutation：N212Q, A298V NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 8000, 200 mM NaCI, 100 mM citrate-phosphate buffer pH 5
Resolution 2.70 Å R-free 0.286
6NMY A Cytokine-receptor complex Deposited 2019-01-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 20–307（288 aa）
Mutation：N194Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；277.15 K；Crystals were grown in 10 mM Tris pH6.8, 8% PEG 8000, 0.15 M magnesium chloride
Resolution 3.30 Å R-free 0.278
6NMY A Cytokine-receptor complex Deposited 2019-01-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain M 20–307（288 aa）
Mutation：N194Q NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；277.15 K；Crystals were grown in 10 mM Tris pH6.8, 8% PEG 8000, 0.15 M magnesium chloride
Resolution 3.30 Å R-free 0.278

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

View Construct and Data Evidence
UniProt name IL3RA_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain G； PDBConstruct 1–288； UniProt 20–307

Interleukin-3

Homo sapiens

UniProt P08700

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 × 2 其他Polymer 1 PDB declaration: dimeric（2） Consistent with protein copy count Chain I； UniProt 31–152 Fragment：UNP residues 31-152 Mutation：W32Y, K116W Interleukin-3 receptor subunit alpha × 1 （P26951） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CIT CITRIC ACID × 2 IMD IMIDAZOLE × 1 EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；20% PEG 8000, 200 mM NaCl and 100 mM citrate-phosphate buffer pH 4.8 Resolution 2.40 Å R-free 0.242

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.

Other PDB Difference from Current Entry 5UWC Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1JLI HUMAN INTERLEUKIN 3 (IL-3) MUTANT WITH TRUNCATION AT BOTH N-AND C-TERMINI AND 14 RESIDUE CHANGES, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1995-12-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 34–144（111 aa）
Mutation：DEL(1-13), V14A, N18I, T25H, Q29R, L32N, F37P, G42S, Q45M, N51R, R55T, E59L, N62V, S67H, Q69E, DEL(126-133) No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
5UV8 Interleukin-3 Receptor Complex Deposited 2017-02-19 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 31–152（122 aa） Fragment：UNP residues 31-152
Mutation：W32Y NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 8000, 200 mM NaCI, 100 mM citrate-phosphate buffer pH 5
Resolution 2.70 Å R-free 0.286
5UV8 Interleukin-3 Receptor Complex Deposited 2017-02-19 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 31–152（122 aa） Fragment：UNP residues 31-152
Mutation：W32Y NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 8000, 200 mM NaCI, 100 mM citrate-phosphate buffer pH 5
Resolution 2.70 Å R-free 0.286
6NMY A Cytokine-receptor complex Deposited 2019-01-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain J 31–144（114 aa）
Mutation：W13Y No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；277.15 K；Crystals were grown in 10 mM Tris pH6.8, 8% PEG 8000, 0.15 M magnesium chloride
Resolution 3.30 Å R-free 0.278
6NMY A Cytokine-receptor complex Deposited 2019-01-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain I 31–144（114 aa）
Mutation：W13Y NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；277.15 K；Crystals were grown in 10 mM Tris pH6.8, 8% PEG 8000, 0.15 M magnesium chloride
Resolution 3.30 Å R-free 0.278

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

View Construct and Data Evidence
UniProt name IL3_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain I； PDBConstruct 1–122； UniProt 31–152

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 5uwc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5uwc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5uwc
Deposition date deposition_date2017-02-21
Structure title titleCytokine-receptor complex
Keywords keywordsCytokine, Receptor, Signalling, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier24.96 Å
Radius of gyration Rg (electron density) rg_electron24.25 Å
Forward intensity I(0) i033399800.00
Molecular weight molecular_weight43568.0 kDa
Excluded volume excluded_volume54153 ų
Envelope volume envelope_volume67922 ų
Hydration-shell volume shell_volume24130 ų
Envelope diameter envelope_diameter88.8 Å
Shell Rg shell_rg30.42 Å
Envelope Rg envelope_rg24.67 Å
Shape Rg shape_rg24.21 Å
Total Rg total_rg25.12 Å
Total atoms total_atoms3061
Residues n_residues365
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax87.7 Å
Rg (real space) rg_real25.01 Å
Rg uncertainty (real space) rg_real_error0.75 Å
I(0) (real space) i0_real3.3400e+07
I(0) uncertainty (real space) i0_real_error5.0110e+05
Rg (reciprocal space) rg_reciprocal25.00 Å
I(0) (reciprocal space) i0_reciprocal33400000.0000
Solution quality estimate total_estimate0.5928
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary29.2 Å
Skewness Skewness skewness0.403
Kurtosis Kurtosis kurtosis-0.196
Angular range angular_range— – 0.3200 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13510000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.765; Stabil: 0.996; Sysdev: 0.184; Positv: 1.000; Valcen: 0.869; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (8)

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7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5uwci_
Class classa — All alpha proteins
Fold Fold folda.26 — 4-helical cytokines
Superfamily Superfamily superfamilya.26.1 — 4-helical cytokines
Family Family familya.26.1.2 — Short-chain cytokines

CATH v4.4 (4 domains)

Domain ID domain_id5uwcG01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily3850 —
Domain ID domain_id5uwcG02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5uwcG03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5uwcI00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10 —
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8. Citations (1)

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9. Files and Curves (10)