2jz3

SOCS box elonginBC ternary complex

Method: SOLUTION NMR Dmax: 51.3 Å Quality: REASONABLE

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

Suppressor of cytokine signaling 3

Mus musculus

UniProt O35718

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 186–225 Fragment:SOCS box, UNP residues 186-225 Transcription elongation factor B polypeptide 2 × 1 (Q15370) Transcription elongation factor B polypeptide 1 × 1 (P83940) SOLUTION NMR NMR measurement conditions:pH 6.7;310 K;Ionic strength (raw mmCIF value) 0.05;Pressure ambient NMR sample composition:1mM [U-100% 13C; U-100% 15N] socs box; 1mM elonginB; 1mM elonginC; 50mM potassium chloride; 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SOCS3_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–40; UniProt 186–225

Transcription elongation factor B polypeptide 2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–118 Not recorded Suppressor of cytokine signaling 3 × 1 (O35718) Transcription elongation factor B polypeptide 1 × 1 (P83940) SOLUTION NMR NMR measurement conditions:pH 6.7;310 K;Ionic strength (raw mmCIF value) 0.05;Pressure ambient NMR sample composition:1mM [U-100% 13C; U-100% 15N] socs box; 1mM elonginB; 1mM elonginC; 50mM potassium chloride; 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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
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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 17–112 Fragment:UNP residues 17-112 Suppressor of cytokine signaling 3 × 1 (O35718) Transcription elongation factor B polypeptide 2 × 1 (Q15370) SOLUTION NMR NMR measurement conditions:pH 6.7;310 K;Ionic strength (raw mmCIF value) 0.05;Pressure ambient NMR sample composition:1mM [U-100% 13C; U-100% 15N] socs box; 1mM elonginB; 1mM elonginC; 50mM potassium chloride; 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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 4 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

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 2jz3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2jz3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2jz3
Deposition date deposition_date2007-12-27
Structure title titleSOCS box elonginBC ternary complex
Keywords keywords;socs proteins, elongins, cytokine signaling, Growth regulation, Phosphoprotein, SH2 domain, Signal transduction inhibitor, Ubl conjugation pathway, Nucleus, Transcription, Transcription regulation, signaling protein, TRANSCRIPTION INHIBITOR-TRANSCRIPTION COMPLEX ;; TRANSCRIPTION INHIBITOR/TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.71
Radius of gyration Rg (electron density) rg_electron18.84
Forward intensity I(0) i03674020000.00
Molecular weight molecular_weight512340.0 kDa
Excluded volume excluded_volume640060 ų
Envelope volume envelope_volume105060 ų
Hydration-shell volume shell_volume33206 ų
Envelope diameter envelope_diameter91.3
Shell Rg shell_rg33.88
Envelope Rg envelope_rg27.10
Shape Rg shape_rg18.84
Total Rg total_rg19.11
Total atoms total_atoms71560
Residues n_residues4580
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 dmax51.3
Rg (real space) rg_real18.77
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real3.4980e+09
I(0) uncertainty (real space) i0_real_error3.0440e+07
Rg (reciprocal space) rg_reciprocal19.70
I(0) (reciprocal space) i0_reciprocal3674000000.0000
Solution quality estimate total_estimate0.6849
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.150
Kurtosis Kurtosis kurtosis-0.499
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha3.7120
Highest regularization parameter α highest_alpha1592000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.998; Stabil: 0.973; Sysdev: 0.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2jz3b_
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_idd2jz3c_
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

CATH v4.4 (2 domains)

Domain ID domain_id2jz3B01
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_id2jz3C00
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)