1alu

HUMAN INTERLEUKIN-6

Method: X-RAY DIFFRACTION Dmax: 57.8 Å Quality: GOOD

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

INTERLEUKIN-6

Homo sapiens

UniProt P05231

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 28–212 Not recorded SO4 SULFATE ION × 8 TLA L(+)-TARTARIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.3;PROTEIN AT 15 MG/ML WAS CRYSTALLIZED FROM 1.8M AMMONIUM SULFATE, 300 MM SODIUM POTASSIUM TARTRATE, IN 100MM PH 6.3 SODIUM CITRATE BUFFER. Resolution 1.90 Å R-free 0.277
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 28–212 Not recorded SO4 SULFATE ION × 8 TLA L(+)-TARTARIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.3;PROTEIN AT 15 MG/ML WAS CRYSTALLIZED FROM 1.8M AMMONIUM SULFATE, 300 MM SODIUM POTASSIUM TARTRATE, IN 100MM PH 6.3 SODIUM CITRATE BUFFER. Resolution 1.90 Å R-free 0.277

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.

16 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–186; UniProt 28–212

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 1alu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1alu
Deposition date deposition_date1997-06-03
Structure title titleHUMAN INTERLEUKIN-6
Keywords keywordsCYTOKINE, INTERLEUKIN, RECEPTOR, SIGNALING, GLYCOPROTEIN; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.28
Radius of gyration Rg (electron density) rg_electron15.83
Forward intensity I(0) i06789250.00
Molecular weight molecular_weight18370.0 kDa
Excluded volume excluded_volume22772 ų
Envelope volume envelope_volume26557 ų
Hydration-shell volume shell_volume14337 ų
Envelope diameter envelope_diameter53.0
Shell Rg shell_rg21.42
Envelope Rg envelope_rg16.01
Shape Rg shape_rg15.81
Total Rg total_rg16.87
Total atoms total_atoms1278
Residues n_residues157
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 dmax57.8
Rg (real space) rg_real17.19
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real6.7890e+06
I(0) uncertainty (real space) i0_real_error8.7940e+04
Rg (reciprocal space) rg_reciprocal17.20
I(0) (reciprocal space) i0_reciprocal6789000.0000
Solution quality estimate total_estimate0.8053
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.3
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.463
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha874800.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1alua_
Class classa — All alpha proteins
Fold Fold folda.26 — 4-helical cytokines
Superfamily Superfamily superfamilya.26.1 — 4-helical cytokines
Family Family familya.26.1.1 — Long-chain cytokines

CATH v4.4 (1 domains)

Domain ID domain_id1aluA00
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)