8sv8

Cryo-EM structure of a double loaded human UBA7-UBE2L6-ISG15 thioester mimetic complex from a composite map

Method: ELECTRON MICROSCOPY Dmax: 110.6 Å Quality: REASONABLE

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1012 Not recorded Ubiquitin-like protein ISG15 × 2 (P05161) Ubiquitin/ISG15-conjugating enzyme E2 L6 × 1 (O14933) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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 1–1012; 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–157 Chain D; UniProt 1–157 Mutation:C78S 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 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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 B; PDBConstruct 1–157; UniProt 1–157 Author chain D; 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 2–153 Mutation:C98S/C102S/L121K Ubiquitin-like modifier-activating enzyme 7 × 1 (P41226) Ubiquitin-like protein ISG15 × 2 (P05161) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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 C; PDBConstruct 1–152; UniProt 2–153

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 8sv8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8sv8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8sv8
Deposition date deposition_date2023-05-15
Structure title titleCryo-EM structure of a double loaded human UBA7-UBE2L6-ISG15 thioester mimetic complex from a composite map
Keywords keywordsComplex, ubiquitin, ligase, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.13
Radius of gyration Rg (electron density) rg_electron34.31
Forward intensity I(0) i0319176000.00
Molecular weight molecular_weight144710.0 kDa
Excluded volume excluded_volume181550 ų
Envelope volume envelope_volume240790 ų
Hydration-shell volume shell_volume56924 ų
Envelope diameter envelope_diameter110.8
Shell Rg shell_rg42.35
Envelope Rg envelope_rg33.71
Shape Rg shape_rg34.32
Total Rg total_rg34.88
Total atoms total_atoms10208
Residues n_residues1299
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 dmax110.6
Rg (real space) rg_real34.96
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real3.1920e+08
I(0) uncertainty (real space) i0_real_error4.9740e+06
Rg (reciprocal space) rg_reciprocal35.07
I(0) (reciprocal space) i0_reciprocal319200000.0000
Solution quality estimate total_estimate0.7104
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.2
Skewness Skewness skewness0.167
Kurtosis Kurtosis kurtosis-0.506
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha68790000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 0.186; Positv: 1.000; Valcen: 0.985; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)