8v29

Cryo-EM structure of human type I OSM receptor complex: model for full extracellular assembly

Method: ELECTRON MICROSCOPY Dmax: 200.9 Å Quality: GOOD

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

Oncostatin-M

Homo sapiens

UniProt P13725

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 Heteromer Protein × 3 其他Polymer 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 26–221 Not recorded Interleukin-6 receptor subunit beta × 1 (P40189) Leukemia inhibitory factor receptor × 1 (P42702) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ONCM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–196; UniProt 26–221

Interleukin-6 receptor subunit beta

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 Other combination Heteromer Protein × 3 其他Polymer 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 23–619 Not recorded Oncostatin-M × 1 (P13725) Leukemia inhibitory factor receptor × 1 (P42702) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 Å

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–597; UniProt 23–619

Leukemia inhibitory factor receptor

Homo sapiens

UniProt P42702

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 Heteromer Protein × 3 其他Polymer 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 45–833 Not recorded Oncostatin-M × 1 (P13725) Interleukin-6 receptor subunit beta × 1 (P40189) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 Å

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LIFR_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–789; UniProt 45–833

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 8v29

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v29
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8v29
Deposition date deposition_date2023-11-22
Structure title titleCryo-EM structure of human type I OSM receptor complex: model for full extracellular assembly
Keywords keywordscytokine signaling, OSM, gp130, LIFR, CYTOKINE, CYTOKINE-RECEPTOR complex; CYTOKINE/RECEPTOR
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.84
Radius of gyration Rg (electron density) rg_electron63.06
Forward intensity I(0) i0446709000.00
Molecular weight molecular_weight176920.0 kDa
Excluded volume excluded_volume221690 ų
Envelope volume envelope_volume421010 ų
Hydration-shell volume shell_volume60257 ų
Envelope diameter envelope_diameter225.9
Shell Rg shell_rg58.92
Envelope Rg envelope_rg60.01
Shape Rg shape_rg63.07
Total Rg total_rg62.89
Total atoms total_atoms12457
Residues n_residues1524
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 dmax200.9
Rg (real space) rg_real63.12
Rg uncertainty (real space) rg_real_error1.64
I(0) (real space) i0_real4.4660e+08
I(0) uncertainty (real space) i0_real_error7.4820e+06
Rg (reciprocal space) rg_reciprocal62.52
I(0) (reciprocal space) i0_reciprocal446200000.0000
Solution quality estimate total_estimate0.8427
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary80.3
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha17080000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.221

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)