5eql

Isoform-specific inhibition of SUMO-dependent protein-protein interactions

Method: X-RAY DIFFRACTION Dmax: 62.1 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 B; UniProt 14–89 Fragment:UNP residues 14-89 SUMO-Affirmer-S2D5 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.6;291 K;0.1 M HEPES sodium salt pH 7.6, 22% w/v polyethylene glycol 3350 Resolution 2.49 Å R-free 0.243

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 2
Chains and sequence ranges Author chain B; PDBConstruct 2–77; UniProt 14–89

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 5eql

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5eql
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5eql
Deposition date deposition_date2015-11-13
Structure title titleIsoform-specific inhibition of SUMO-dependent protein-protein interactions
Keywords keywordsUbiquitin, Sumoylation, protein binding; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.70
Radius of gyration Rg (electron density) rg_electron17.67
Forward intensity I(0) i05903680.00
Molecular weight molecular_weight17464.0 kDa
Excluded volume excluded_volume21746 ų
Envelope volume envelope_volume26141 ų
Hydration-shell volume shell_volume13317 ų
Envelope diameter envelope_diameter61.8
Shell Rg shell_rg22.37
Envelope Rg envelope_rg17.86
Shape Rg shape_rg17.68
Total Rg total_rg18.45
Total atoms total_atoms1232
Residues n_residues158
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 dmax62.1
Rg (real space) rg_real18.78
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real5.9040e+06
I(0) uncertainty (real space) i0_real_error7.6360e+04
Rg (reciprocal space) rg_reciprocal18.77
I(0) (reciprocal space) i0_reciprocal5904000.0000
Solution quality estimate total_estimate0.8722
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.3
Skewness Skewness skewness0.449
Kurtosis Kurtosis kurtosis-0.312
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1667000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5eqlA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)