6i4x

Crystal structure of SOCS2:Elongin C:Elongin B in complex with erythropoietin receptor peptide

Method: X-RAY DIFFRACTION Dmax: 93.3 Å Quality: REASONABLE

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

Elongin-B

Homo sapiens

UniProt Q15370

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–104 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-C × 1 (Q15369) Suppressor of cytokine signaling 2 × 1 (O14508) Erythropoietin receptor × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;Sodium cacodylate, ethanol, HEPES, magnesium chloride Resolution 2.69 Å R-free 0.235

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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform Q15370-2
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–104; UniProt 1–104

Elongin-C

Homo sapiens

UniProt Q15369

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 17–112 Not recorded Elongin-B × 1 (Q15370) Suppressor of cytokine signaling 2 × 1 (O14508) Erythropoietin receptor × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;Sodium cacodylate, ethanol, HEPES, magnesium chloride Resolution 2.69 Å R-free 0.235

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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–97; UniProt 17–112

Suppressor of cytokine signaling 2

Homo sapiens

UniProt O14508

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 30–198 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Erythropoietin receptor × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;Sodium cacodylate, ethanol, HEPES, magnesium chloride Resolution 2.69 Å R-free 0.235

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.

12 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SOCS2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–169; UniProt 30–198

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 6i4x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6i4x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6i4x
Deposition date deposition_date2018-11-12
Structure title titleCrystal structure of SOCS2:Elongin C:Elongin B in complex with erythropoietin receptor peptide
Keywords keywordsComplex, 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_guinier24.79
Radius of gyration Rg (electron density) rg_electron23.88
Forward intensity I(0) i025137800.00
Molecular weight molecular_weight39526.0 kDa
Excluded volume excluded_volume49921 ų
Envelope volume envelope_volume60381 ų
Hydration-shell volume shell_volume22006 ų
Envelope diameter envelope_diameter89.8
Shell Rg shell_rg30.05
Envelope Rg envelope_rg24.09
Shape Rg shape_rg23.88
Total Rg total_rg24.68
Total atoms total_atoms2771
Residues n_residues353
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 dmax93.3
Rg (real space) rg_real24.92
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real2.5140e+07
I(0) uncertainty (real space) i0_real_error3.5460e+05
Rg (reciprocal space) rg_reciprocal24.89
I(0) (reciprocal space) i0_reciprocal25140000.0000
Solution quality estimate total_estimate0.7277
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.458
Kurtosis Kurtosis kurtosis-0.268
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5350000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.618; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.601; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6i4xA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology750 — Elongin C; Chain C, domain 1
Homologous superfamily homologous superfamily20 — SOCS box
Domain ID domain_id6i4xB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id6i4xC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A

8. Citations (1)

9. Files and Curves (10)