1m48

Crystal Structure of Human IL-2 Complexed with (R)-N-[2-[1-(Aminoiminomethyl)-3-piperidinyl]-1-oxoethyl]-4-(phenylethynyl)-L-phenylalanine methyl ester

Method: X-RAY DIFFRACTION Dmax: 70.0 Å Quality: GOOD

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

interleukin-2

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 21–153 Not recorded FRG 2-[3-METHYL-4-(N-METHYL-GUANIDINO)-BUTYRYLAMINO]-3-(4-PHENYLETHYNYL-PHENYL)-PROPIONIC ACID METHYL ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.95 Å R-free 0.269
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 21–153 Not recorded FRG 2-[3-METHYL-4-(N-METHYL-GUANIDINO)-BUTYRYLAMINO]-3-(4-PHENYLETHYNYL-PHENYL)-PROPIONIC ACID METHYL ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.95 Å R-free 0.269

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 76 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 1–133; UniProt 21–153 Author chain B; PDBConstruct 1–133; UniProt 21–153

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 1m48

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1m48
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1m48
Deposition date deposition_date2002-07-02
Structure title titleCrystal Structure of Human IL-2 Complexed with (R)-N-[2-[1-(Aminoiminomethyl)-3-piperidinyl]-1-oxoethyl]-4-(phenylethynyl)-L-phenylalanine methyl ester
Keywords keywordsinterleukin-2, four-helix bundle, small molecule complex, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.07
Radius of gyration Rg (electron density) rg_electron20.13
Forward intensity I(0) i014059100.00
Molecular weight molecular_weight29736.0 kDa
Excluded volume excluded_volume37973 ų
Envelope volume envelope_volume44940 ų
Hydration-shell volume shell_volume19154 ų
Envelope diameter envelope_diameter70.8
Shell Rg shell_rg25.82
Envelope Rg envelope_rg20.30
Shape Rg shape_rg20.13
Total Rg total_rg20.98
Total atoms total_atoms2087
Residues n_residues249
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 dmax70.0
Rg (real space) rg_real21.04
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.4060e+07
I(0) uncertainty (real space) i0_real_error1.7400e+05
Rg (reciprocal space) rg_reciprocal21.05
I(0) (reciprocal space) i0_reciprocal14060000.0000
Solution quality estimate total_estimate0.8843
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2633000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1m48a_
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
Domain ID domain_idd1m48b_
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 (2 domains)

Domain ID domain_id1m48A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10
Domain ID domain_id1m48B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)