8d7r

Cryo-EM structure of human CLCF1 signaling complex: model containing the interaction core region

Method: ELECTRON MICROSCOPY Dmax: 161.7 Å Quality: GOOD

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

Cardiotrophin-like cytokine factor 1

Homo sapiens

UniProt Q9UBD9

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 × 4 其他Polymer 5 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 28–225 Not recorded Ciliary neurotrophic factor receptor subunit alpha × 1 (P26992) Leukemia inhibitory factor receptor × 1 (P42702) 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CLCF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–198; UniProt 28–225

Ciliary neurotrophic factor receptor subunit alpha

Homo sapiens

UniProt P26992

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 × 4 其他Polymer 5 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 23–346 Not recorded Cardiotrophin-like cytokine factor 1 × 1 (Q9UBD9) Leukemia inhibitory factor receptor × 1 (P42702) 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNTFR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–324; UniProt 23–346

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 × 4 其他Polymer 5 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 45–833 Not recorded Cardiotrophin-like cytokine factor 1 × 1 (Q9UBD9) Ciliary neurotrophic factor receptor subunit alpha × 1 (P26992) 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 B; PDBConstruct 1–789; UniProt 45–833

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 × 4 其他Polymer 5 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 23–619 Not recorded Cardiotrophin-like cytokine factor 1 × 1 (Q9UBD9) Ciliary neurotrophic factor receptor subunit alpha × 1 (P26992) 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 4
Chains and sequence ranges Author chain A; PDBConstruct 1–597; UniProt 23–619

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 8d7r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8d7r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8d7r
Deposition date deposition_date2022-06-07
Structure title titleCryo-EM structure of human CLCF1 signaling complex: model containing the interaction core region
Keywords keywordscytokine signaling, CLCF1, CNTFR alpha, gp130, LIFR, CYTOKINE; CYTOKINE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.97
Radius of gyration Rg (electron density) rg_electron48.28
Forward intensity I(0) i0268885000.00
Molecular weight molecular_weight136410.0 kDa
Excluded volume excluded_volume171660 ų
Envelope volume envelope_volume285750 ų
Hydration-shell volume shell_volume52595 ų
Envelope diameter envelope_diameter171.9
Shell Rg shell_rg48.33
Envelope Rg envelope_rg47.26
Shape Rg shape_rg48.27
Total Rg total_rg48.32
Total atoms total_atoms9627
Residues n_residues1167
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 dmax161.7
Rg (real space) rg_real48.21
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real2.6890e+08
I(0) uncertainty (real space) i0_real_error5.5530e+06
Rg (reciprocal space) rg_reciprocal47.97
I(0) (reciprocal space) i0_reciprocal268800000.0000
Solution quality estimate total_estimate0.8681
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary53.9
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.306
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12550000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.675

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8d7rD01
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)