6jxx

SUMO2 bound to phosphorylated SLS4-SIM peptide from ICP0

Method: SOLUTION NMR Dmax: 43.0 Å Quality: GOOD

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

Small ubiquitin-related modifier 2

Homo sapiens

UniProt P61956

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–95 Not recorded Phosphorylated SLS4 from E3 ubiquitin ligase ICP0 × 1 SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Ionic strength (raw mmCIF value) 137;Pressure 1 NMR sample composition:0.5 mM [U-15N] SUMO2, 2 mM Phosphorylated SLS4 from E3 ubiquitin ligase ICP0, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.7 mM [U-13C; U-15N] SUMO2, 1.5 mM Phosphorylated SLS4 from E3 ubiquitin ligase ICP0, 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.

24 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUMO2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–95; UniProt 1–95

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 6jxx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6jxx
Deposition date deposition_date2019-04-25
Structure title titleSUMO2 bound to phosphorylated SLS4-SIM peptide from ICP0
Keywords keywordsSUMOylation, Phosphorylation, Protein-Binding-peptide complex, PROTEIN BINDING-PEPTIDE complex; PROTEIN BINDING/PEPTIDE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.37
Radius of gyration Rg (electron density) rg_electron12.70
Forward intensity I(0) i0695079000.00
Molecular weight molecular_weight206630.0 kDa
Excluded volume excluded_volume252040 ų
Envelope volume envelope_volume19640 ų
Hydration-shell volume shell_volume12157 ų
Envelope diameter envelope_diameter49.5
Shell Rg shell_rg19.55
Envelope Rg envelope_rg14.14
Shape Rg shape_rg12.69
Total Rg total_rg12.85
Total atoms total_atoms28340
Residues n_residues1740
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 dmax43.0
Rg (real space) rg_real13.28
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real6.9510e+08
I(0) uncertainty (real space) i0_real_error7.1770e+06
Rg (reciprocal space) rg_reciprocal13.29
I(0) (reciprocal space) i0_reciprocal695100000.0000
Solution quality estimate total_estimate0.8739
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.9
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.250
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha225800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)