9lhj

UBE2N/UBE2V2 complexed with a covalent inhibitor

Method: X-RAY DIFFRACTION Dmax: 91.6 Å Quality: EXCELLENT

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

Ubiquitin-conjugating enzyme E2 N

Homo sapiens

UniProt P61088

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 1–152 Non-standard monomer:Yes (specific site not provided by mmCIF) Ubiquitin-conjugating enzyme E2 variant 2 × 1 (Q15819) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289.15 K;0.1 M BIS-TRIS pH 6.5, 20% w/v PEG 5,000 Resolution 1.68 Å R-free 0.228
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–152 Non-standard monomer:Yes (specific site not provided by mmCIF) Ubiquitin-conjugating enzyme E2 variant 2 × 1 (Q15819) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289.15 K;0.1 M BIS-TRIS pH 6.5, 20% w/v PEG 5,000 Resolution 1.68 Å R-free 0.228

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.

43 other PDB entries and 72 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBE2N_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–152; UniProt 1–152 Author chain B; PDBConstruct 1–152; UniProt 1–152

Ubiquitin-conjugating enzyme E2 variant 2

Homo sapiens

UniProt Q15819

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 D; UniProt 1–145 Not recorded Ubiquitin-conjugating enzyme E2 N × 1 (P61088) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289.15 K;0.1 M BIS-TRIS pH 6.5, 20% w/v PEG 5,000 Resolution 1.68 Å R-free 0.228
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–145 Not recorded Ubiquitin-conjugating enzyme E2 N × 1 (P61088) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289.15 K;0.1 M BIS-TRIS pH 6.5, 20% w/v PEG 5,000 Resolution 1.68 Å R-free 0.228

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.

17 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2V2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–145; UniProt 1–145 Author chain D; PDBConstruct 1–145; UniProt 1–145

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 9lhj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9lhj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9lhj
Deposition date deposition_date2025-01-12
Structure title titleUBE2N/UBE2V2 complexed with a covalent inhibitor
Keywords keywordsCovalent inhibitor, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.29
Radius of gyration Rg (electron density) rg_electron29.66
Forward intensity I(0) i0131925000.00
Molecular weight molecular_weight60903.0 kDa
Excluded volume excluded_volume59092 ų
Envelope volume envelope_volume109890 ų
Hydration-shell volume shell_volume31647 ų
Envelope diameter envelope_diameter100.5
Shell Rg shell_rg35.97
Envelope Rg envelope_rg29.12
Shape Rg shape_rg29.63
Total Rg total_rg30.18
Total atoms total_atoms4673
Residues n_residues567
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 dmax91.6
Rg (real space) rg_real30.17
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.3190e+08
I(0) uncertainty (real space) i0_real_error1.8680e+06
Rg (reciprocal space) rg_reciprocal30.23
I(0) (reciprocal space) i0_reciprocal131900000.0000
Solution quality estimate total_estimate0.9132
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.3
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.683
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11360000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.979; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)