4jgh

Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5

Method: X-RAY DIFFRACTION Dmax: 126.4 Å Quality: GOOD

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

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 32–198 Fragment:unp residues 32-198 Transcription elongation factor B polypeptide 2 × 1 (P62869) Transcription elongation factor B polypeptide 1 × 1 (P83940) Cullin-5 × 1 (Q93034) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295.15 K;0.25 M sodium citrate and 18 % (w/v) PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K Resolution 3.00 Å R-free 0.248
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 32–198 Fragment:unp residues 32-198 Transcription elongation factor B polypeptide 2 × 1 (P62869) Transcription elongation factor B polypeptide 1 × 1 (P83940) Cullin-5 × 1 (Q93034) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295.15 K;0.25 M sodium citrate and 18 % (w/v) PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K Resolution 3.00 Å R-free 0.248

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 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SOCS2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–173; UniProt 32–198

Transcription elongation factor B polypeptide 2

Mus musculus

UniProt P62869

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 1–118 Not recorded Suppressor of cytokine signaling 2 × 1 (O14508) Transcription elongation factor B polypeptide 1 × 1 (P83940) Cullin-5 × 1 (Q93034) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295.15 K;0.25 M sodium citrate and 18 % (w/v) PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K Resolution 3.00 Å R-free 0.248
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–118 Not recorded Suppressor of cytokine signaling 2 × 1 (O14508) Transcription elongation factor B polypeptide 1 × 1 (P83940) Cullin-5 × 1 (Q93034) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295.15 K;0.25 M sodium citrate and 18 % (w/v) PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K Resolution 3.00 Å R-free 0.248

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 ELOB_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–118; UniProt 1–118

Transcription elongation factor B polypeptide 1

Mus musculus

UniProt P83940

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 Fragment:unp residues 17-112 Suppressor of cytokine signaling 2 × 1 (O14508) Transcription elongation factor B polypeptide 2 × 1 (P62869) Cullin-5 × 1 (Q93034) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295.15 K;0.25 M sodium citrate and 18 % (w/v) PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K Resolution 3.00 Å R-free 0.248
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 17–112 Fragment:unp residues 17-112 Suppressor of cytokine signaling 2 × 1 (O14508) Transcription elongation factor B polypeptide 2 × 1 (P62869) Cullin-5 × 1 (Q93034) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295.15 K;0.25 M sodium citrate and 18 % (w/v) PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K Resolution 3.00 Å R-free 0.248

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–96; UniProt 17–112

Cullin-5

Homo sapiens

UniProt Q93034

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 D; UniProt 10–386 Fragment:unp residues 10-386 Mutation:V341R, L345D Suppressor of cytokine signaling 2 × 1 (O14508) Transcription elongation factor B polypeptide 2 × 1 (P62869) Transcription elongation factor B polypeptide 1 × 1 (P83940) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295.15 K;0.25 M sodium citrate and 18 % (w/v) PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K Resolution 3.00 Å R-free 0.248
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 10–386 Fragment:unp residues 10-386 Mutation:V341R, L345D Suppressor of cytokine signaling 2 × 1 (O14508) Transcription elongation factor B polypeptide 2 × 1 (P62869) Transcription elongation factor B polypeptide 1 × 1 (P83940) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295.15 K;0.25 M sodium citrate and 18 % (w/v) PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K Resolution 3.00 Å R-free 0.248

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.

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

View Construct and Data Evidence
UniProt name CUL5_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–377; UniProt 10–386

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 4jgh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4jgh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4jgh
Deposition date deposition_date2013-03-01
Structure title titleStructure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5
Keywords keywordsCullin-RING E3 ubiquitin ligases, Ubiquitination, Cytosol, ligase; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.62
Radius of gyration Rg (electron density) rg_electron38.23
Forward intensity I(0) i0105481000.00
Molecular weight molecular_weight83942.0 kDa
Excluded volume excluded_volume105630 ų
Envelope volume envelope_volume155950 ų
Hydration-shell volume shell_volume34782 ų
Envelope diameter envelope_diameter127.2
Shell Rg shell_rg43.34
Envelope Rg envelope_rg37.84
Shape Rg shape_rg38.21
Total Rg total_rg38.63
Total atoms total_atoms5902
Residues n_residues731
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 dmax126.4
Rg (real space) rg_real38.74
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real1.0550e+08
I(0) uncertainty (real space) i0_real_error1.8540e+06
Rg (reciprocal space) rg_reciprocal38.67
I(0) (reciprocal space) i0_reciprocal105500000.0000
Solution quality estimate total_estimate0.8728
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.8
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.761
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7857000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.854; Smooth: 0.804

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd4jgha1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.93 — SH2-like
Superfamily Superfamily superfamilyd.93.1 — SH2 domain
Family Family familyd.93.1.1 — SH2 domain
Domain ID domain_idd4jgha2
Class classa — All alpha proteins
Fold Fold folda.271 — SOCS box-like
Superfamily Superfamily superfamilya.271.1 — SOCS box-like
Family Family familya.271.1.0 — automated matches
Domain ID domain_idd4jgha3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4jghb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd4jghc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.1 — BTB/POZ domain
Domain ID domain_idd4jghd1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.17 — Cullin repeat-like
Family Family familya.118.17.0 — automated matches
Domain ID domain_idd4jghd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (7 domains)

Domain ID domain_id4jghA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
Domain ID domain_id4jghA02
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_id4jghB00
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_id4jghC00
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
Domain ID domain_id4jghD01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id4jghD02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id4jghD03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats

8. Citations (1)

9. Files and Curves (10)