7un3

Complex of UBE2O with NAP1L1 and ubiquitylated uL2

Method: ELECTRON MICROSCOPY Dmax: 136.1 Å Quality: REASONABLE

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

Ubiquitin,60S ribosomal protein L8,(E3-independent) E2 ubiquitin-conjugating enzyme fusion

Homo sapiens

UniProt P62917

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–257 Chain D; UniProt 1–257 Not recorded Nucleosome assembly protein 1-like 1 × 2 (P55209) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

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.

159 other PDB entries and 159 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 126–382; UniProt 1–257 Author chain D; PDBConstruct 126–382; UniProt 1–257

Ubiquitin,60S ribosomal protein L8,(E3-independent) E2 ubiquitin-conjugating enzyme fusion

Homo sapiens

UniProt P62987

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–76 Chain D; UniProt 1–76 Not recorded Nucleosome assembly protein 1-like 1 × 2 (P55209) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

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.

153 other PDB entries and 174 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL40_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 48–123; UniProt 1–76 Author chain D; PDBConstruct 48–123; UniProt 1–76

Ubiquitin,60S ribosomal protein L8,(E3-independent) E2 ubiquitin-conjugating enzyme fusion

Homo sapiens

UniProt Q9C0C9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1292 Chain D; UniProt 1–1292 Not recorded Nucleosome assembly protein 1-like 1 × 2 (P55209) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBE2O_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 453–1744; UniProt 1–1292 Author chain D; PDBConstruct 453–1744; UniProt 1–1292

Nucleosome assembly protein 1-like 1

Homo sapiens

UniProt P55209

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 2–391 Chain C; UniProt 2–391 Not recorded Ubiquitin,60S ribosomal protein L8,(E3-independent) E2 ubiquitin-conjugating enzyme fusion × 2 (P62987,P62917,Q9C0C9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å

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 NP1L1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 27–416; UniProt 2–391 Author chain C; PDBConstruct 27–416; UniProt 2–391

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 7un3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7un3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7un3
Deposition date deposition_date2022-04-08
Structure title titleComplex of UBE2O with NAP1L1 and ubiquitylated uL2
Keywords keywordsUbiquitylation, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.41
Radius of gyration Rg (electron density) rg_electron43.38
Forward intensity I(0) i0251959000.00
Molecular weight molecular_weight133590.0 kDa
Excluded volume excluded_volume168850 ų
Envelope volume envelope_volume254630 ų
Hydration-shell volume shell_volume50836 ų
Envelope diameter envelope_diameter139.5
Shell Rg shell_rg46.95
Envelope Rg envelope_rg41.48
Shape Rg shape_rg43.36
Total Rg total_rg43.64
Total atoms total_atoms9423
Residues n_residues1164
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 dmax136.1
Rg (real space) rg_real44.69
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.4910e+08
I(0) uncertainty (real space) i0_real_error4.1410e+06
Rg (reciprocal space) rg_reciprocal43.41
I(0) (reciprocal space) i0_reciprocal251900000.0000
Solution quality estimate total_estimate0.6732
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.4
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.645
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha2.5760
Highest regularization parameter α highest_alpha13810000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.971; Stabil: 0.914; Sysdev: 0.000; Positv: 1.000; Valcen: 0.934; Smooth: 0.179

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)