1bbn

THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Method: SOLUTION NMR Dmax: 56.7 Å Quality: GOOD

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

INTERLEUKIN-4

Homo sapiens

UniProt P05112

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 25–153 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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.

27 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–133; UniProt 25–153

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 1bbn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bbn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bbn
Deposition date deposition_date1992-05-01
Structure title titleTHREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Keywords keywordsCYTOKINE; CYTOKINE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.90
Radius of gyration Rg (electron density) rg_electron15.44
Forward intensity I(0) i05010580.00
Molecular weight molecular_weight15369.0 kDa
Excluded volume excluded_volume19109 ų
Envelope volume envelope_volume24328 ų
Hydration-shell volume shell_volume13539 ų
Envelope diameter envelope_diameter58.5
Shell Rg shell_rg21.02
Envelope Rg envelope_rg16.01
Shape Rg shape_rg15.42
Total Rg total_rg16.65
Total atoms total_atoms2157
Residues n_residues133
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 dmax56.7
Rg (real space) rg_real16.85
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real5.0110e+06
I(0) uncertainty (real space) i0_real_error6.1580e+04
Rg (reciprocal space) rg_reciprocal16.85
I(0) (reciprocal space) i0_reciprocal5011000.0000
Solution quality estimate total_estimate0.7940
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.289
Kurtosis Kurtosis kurtosis-0.168
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1047000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.773; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bbna_
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 (1 domains)

Domain ID domain_id1bbnA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10

8. Citations (3)

9. Files and Curves (10)