1n26

Crystal Structure of the extra-cellular domains of Human Interleukin-6 Receptor alpha chain

Method: X-RAY DIFFRACTION Dmax: 108.6 Å Quality: GOOD

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

IL-6 Receptor alpha chain

Homo sapiens

UniProt P08887

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 Homooligomer Protein × 2 其他Polymer 4 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 20–344 Fragment:IL-6R extral-cellular domains ;2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 SO4 SULFATE ION × 4 CYS CYSTEINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;300 K;ammonium sulphate, PEG 3350, sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 300K Resolution 2.40 Å R-free 0.290

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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL6A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–325; UniProt 20–344

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 1n26

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1n26
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1n26
Deposition date deposition_date2002-10-22
Structure title titleCrystal Structure of the extra-cellular domains of Human Interleukin-6 Receptor alpha chain
Keywords keywordsTransmembrane, Glycoprotein, Immunoglobulin domain, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.07
Radius of gyration Rg (electron density) rg_electron30.19
Forward intensity I(0) i022960900.00
Molecular weight molecular_weight35584.0 kDa
Excluded volume excluded_volume43895 ų
Envelope volume envelope_volume60982 ų
Hydration-shell volume shell_volume19451 ų
Envelope diameter envelope_diameter114.5
Shell Rg shell_rg32.42
Envelope Rg envelope_rg30.35
Shape Rg shape_rg30.21
Total Rg total_rg30.36
Total atoms total_atoms2497
Residues n_residues299
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 dmax108.6
Rg (real space) rg_real30.54
Rg uncertainty (real space) rg_real_error1.33
I(0) (real space) i0_real2.2960e+07
I(0) uncertainty (real space) i0_real_error4.7710e+05
Rg (reciprocal space) rg_reciprocal30.34
I(0) (reciprocal space) i0_reciprocal22960000.0000
Solution quality estimate total_estimate0.7508
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.578
Kurtosis Kurtosis kurtosis-0.350
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2264000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.536; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.248; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1n26a1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains
Domain ID domain_idd1n26a2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III
Domain ID domain_idd1n26a3
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III

CATH v4.4 (3 domains)

Domain ID domain_id1n26A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1n26A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1n26A03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)