1bqu

CYTOKYNE-BINDING REGION OF GP130

Method: X-RAY DIFFRACTION Dmax: 89.2 Å Quality: EXCELLENT

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

PROTEIN (GP130)

Homo sapiens

UniProt P40189

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 119–333 Chain B; UniProt 119–333 Fragment:CYTOKINE-BINDING REGION DOMAINS SO4 SULFATE ION × 6 GOL GLYCEROL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;1.8-2.1M AMMONIUM SULFATE, 0.1M TRIS PH 8.0 Resolution 2.00 Å R-free 0.255

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.

19 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL6RB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–215; UniProt 119–333 Author chain B; PDBConstruct 1–215; UniProt 119–333

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 1bqu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bqu
Deposition date deposition_date1998-08-18
Structure title titleCYTOKYNE-BINDING REGION OF GP130
Keywords keywordsCYTOKINE RECEPTOR, GLYCOPROTEIN 130, GP130, INTERLEUKINE 6 RECEPTOR BETA SUBUNIT, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.96
Radius of gyration Rg (electron density) rg_electron27.15
Forward intensity I(0) i041668100.00
Molecular weight molecular_weight48655.0 kDa
Excluded volume excluded_volume60282 ų
Envelope volume envelope_volume79269 ų
Hydration-shell volume shell_volume25481 ų
Envelope diameter envelope_diameter94.2
Shell Rg shell_rg32.73
Envelope Rg envelope_rg27.60
Shape Rg shape_rg27.19
Total Rg total_rg27.66
Total atoms total_atoms3418
Residues n_residues423
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 dmax89.2
Rg (real space) rg_real27.89
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real4.1670e+07
I(0) uncertainty (real space) i0_real_error5.4380e+05
Rg (reciprocal space) rg_reciprocal27.91
I(0) (reciprocal space) i0_reciprocal41670000.0000
Solution quality estimate total_estimate0.9048
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.1
Skewness Skewness skewness0.162
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5374000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1bqua1
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_idd1bqua2
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_idd1bqub1
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_idd1bqub2
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 (4 domains)

Domain ID domain_id1bquA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1bquA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1bquB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1bquB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)