9qii

Structure of UBA6 (cluster 3)

Method: ELECTRON MICROSCOPY Dmax: 109.6 Å Quality: EXCELLENT

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

Ubiquitin-like modifier-activating enzyme 6

Homo sapiens

UniProt A0AVT1

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–1052 Not recorded IHP INOSITOL HEXAKISPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

13 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBA6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 3–1054; UniProt 1–1052

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 9qii

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qii
Deposition date deposition_date2025-03-17
Structure title titleStructure of UBA6 (cluster 3)
Keywords keywordsE1, Ligase, SIGNALING PROTEIN; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.49
Radius of gyration Rg (electron density) rg_electron33.82
Forward intensity I(0) i0200993000.00
Molecular weight molecular_weight114880.0 kDa
Excluded volume excluded_volume144260 ų
Envelope volume envelope_volume189310 ų
Hydration-shell volume shell_volume46561 ų
Envelope diameter envelope_diameter113.6
Shell Rg shell_rg40.78
Envelope Rg envelope_rg33.31
Shape Rg shape_rg33.83
Total Rg total_rg34.33
Total atoms total_atoms8077
Residues n_residues1011
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 dmax109.6
Rg (real space) rg_real34.37
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real2.0100e+08
I(0) uncertainty (real space) i0_real_error3.1060e+06
Rg (reciprocal space) rg_reciprocal34.45
I(0) (reciprocal space) i0_reciprocal201000000.0000
Solution quality estimate total_estimate0.9039
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.9
Skewness Skewness skewness0.163
Kurtosis Kurtosis kurtosis-0.570
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31070000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.922

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)