8oif

Structure of the UBE1L activating enzyme bound to ISG15 and UBE2L6

Method: ELECTRON MICROSCOPY Dmax: 108.5 Å Quality: GOOD

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

Ubiquitin-like modifier-activating enzyme 7

Homo sapiens

UniProt P41226

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 1–1012 Not recorded Ubiquitin-like protein ISG15 × 1 (P05161) Ubiquitin/ISG15-conjugating enzyme E2 L6 × 1 (O14933) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBA7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–1014; UniProt 1–1012

Ubiquitin-like protein ISG15

Homo sapiens

UniProt P05161

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 I; UniProt 1–157 Not recorded Ubiquitin-like modifier-activating enzyme 7 × 1 (P41226) Ubiquitin/ISG15-conjugating enzyme E2 L6 × 1 (O14933) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

21 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ISG15_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–157; UniProt 1–157

Ubiquitin/ISG15-conjugating enzyme E2 L6

Homo sapiens

UniProt O14933

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 L; UniProt 1–153 Not recorded Ubiquitin-like modifier-activating enzyme 7 × 1 (P41226) Ubiquitin-like protein ISG15 × 1 (P05161) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

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

View Construct and Data Evidence
UniProt name UB2L6_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain L; PDBConstruct 3–155; UniProt 1–153

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 8oif

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8oif
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8oif
Deposition date deposition_date2023-03-22
Structure title titleStructure of the UBE1L activating enzyme bound to ISG15 and UBE2L6
Keywords keywordsubiquitin-like, ISG15, interferon-stimulated genes, antiviral, ANTIVIRAL PROTEIN; ANTIVIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.37
Radius of gyration Rg (electron density) rg_electron32.67
Forward intensity I(0) i0132725000.00
Molecular weight molecular_weight93093.0 kDa
Excluded volume excluded_volume117230 ų
Envelope volume envelope_volume164510 ų
Hydration-shell volume shell_volume42756 ų
Envelope diameter envelope_diameter112.2
Shell Rg shell_rg38.87
Envelope Rg envelope_rg32.37
Shape Rg shape_rg32.69
Total Rg total_rg33.16
Total atoms total_atoms6589
Residues n_residues934
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 dmax108.5
Rg (real space) rg_real33.35
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real1.3270e+08
I(0) uncertainty (real space) i0_real_error2.0030e+06
Rg (reciprocal space) rg_reciprocal33.36
I(0) (reciprocal space) i0_reciprocal132700000.0000
Solution quality estimate total_estimate0.8888
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29050000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.862

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)