6vwu

X-ray structure of ALKS 4230, a fusion of circularly permuted human Interleukin-2 and Interleukin-2 Receptor alpha

Method: X-RAY DIFFRACTION Dmax: 81.4 Å Quality: GOOD

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

Interleukin-2,Interleukin-2 receptor subunit alpha

Homo sapiens

UniProt P01589

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 22–186 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;An equal volume of protein was mixed with crystallization buffer, 25 % (w/v) PEG 3350, 0.2 M MgCl2, 0.1 M Hepes 7.5. Large crystals appeared within 48-72 hours, and were frozen in a cryoprotectant consisting of mother liquor with 10 % glycerol Resolution 3.40 Å R-free 0.297

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.

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

View Construct and Data Evidence
UniProt name IL2RA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 139–303; UniProt 22–186

Interleukin-2,Interleukin-2 receptor subunit alpha

Homo sapiens

UniProt P60568

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 24–94 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;An equal volume of protein was mixed with crystallization buffer, 25 % (w/v) PEG 3350, 0.2 M MgCl2, 0.1 M Hepes 7.5. Large crystals appeared within 48-72 hours, and were frozen in a cryoprotectant consisting of mother liquor with 10 % glycerol Resolution 3.40 Å R-free 0.297

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.

33 other PDB entries and 77 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 62–132; UniProt 24–94

Interleukin-2,Interleukin-2 receptor subunit alpha

Homo sapiens

UniProt Q6QWN0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 75–133 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;An equal volume of protein was mixed with crystallization buffer, 25 % (w/v) PEG 3350, 0.2 M MgCl2, 0.1 M Hepes 7.5. Large crystals appeared within 48-72 hours, and were frozen in a cryoprotectant consisting of mother liquor with 10 % glycerol Resolution 3.40 Å R-free 0.297

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6QWN0_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–59; UniProt 75–133

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 6vwu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6vwu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6vwu
Deposition date deposition_date2020-02-20
Structure title titleX-ray structure of ALKS 4230, a fusion of circularly permuted human Interleukin-2 and Interleukin-2 Receptor alpha
Keywords keywordscircular permutation, ALKS 4230, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.01
Radius of gyration Rg (electron density) rg_electron21.33
Forward intensity I(0) i015963300.00
Molecular weight molecular_weight29421.0 kDa
Excluded volume excluded_volume36610 ų
Envelope volume envelope_volume45500 ų
Hydration-shell volume shell_volume18947 ų
Envelope diameter envelope_diameter81.6
Shell Rg shell_rg26.72
Envelope Rg envelope_rg21.66
Shape Rg shape_rg21.31
Total Rg total_rg22.14
Total atoms total_atoms2057
Residues n_residues258
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 dmax81.4
Rg (real space) rg_real22.15
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.5960e+07
I(0) uncertainty (real space) i0_real_error2.2070e+05
Rg (reciprocal space) rg_reciprocal22.12
I(0) (reciprocal space) i0_reciprocal15960000.0000
Solution quality estimate total_estimate0.8151
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis0.116
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2891000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.631; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.751; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)