9qgw

Consensus structure of UBA6-UbDha-BIRC6 trapped ternary complex (singly loaded)

Method: ELECTRON MICROSCOPY Dmax: 122.3 Å Quality: GOOD

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

Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6

Homo sapiens

UniProt Q9NR09

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 4498–4820 Not recorded Ubiquitin-like modifier-activating enzyme 6 × 1 (A0AVT1) Polyubiquitin-C × 1 (P0CG48) IHP INOSITOL HEXAKISPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.62 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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BIRC6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–325; UniProt 4498–4820

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–1052 Not recorded Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6 × 1 (Q9NR09) Polyubiquitin-C × 1 (P0CG48) IHP INOSITOL HEXAKISPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.62 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 2
Chains and sequence ranges Author chain B; PDBConstruct 3–1054; UniProt 1–1052

Polyubiquitin-C

Homo sapiens

UniProt P0CG48

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 C; UniProt 1–76 Not recorded Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6 × 1 (Q9NR09) Ubiquitin-like modifier-activating enzyme 6 × 1 (A0AVT1) IHP INOSITOL HEXAKISPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.62 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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–76; UniProt 1–76

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 9qgw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qgw
Deposition date deposition_date2025-03-14
Structure title titleConsensus structure of UBA6-UbDha-BIRC6 trapped ternary complex (singly loaded)
Keywords keywordsUbiquitin, E1, E2, Ligase, SIGNALING PROTEIN; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.35
Radius of gyration Rg (electron density) rg_electron36.76
Forward intensity I(0) i0321406000.00
Molecular weight molecular_weight145790.0 kDa
Excluded volume excluded_volume182730 ų
Envelope volume envelope_volume249780 ų
Hydration-shell volume shell_volume55901 ų
Envelope diameter envelope_diameter122.4
Shell Rg shell_rg43.83
Envelope Rg envelope_rg36.00
Shape Rg shape_rg36.75
Total Rg total_rg37.26
Total atoms total_atoms10252
Residues n_residues1282
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 dmax122.3
Rg (real space) rg_real37.27
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real3.2140e+08
I(0) uncertainty (real space) i0_real_error4.8080e+06
Rg (reciprocal space) rg_reciprocal37.32
I(0) (reciprocal space) i0_reciprocal321400000.0000
Solution quality estimate total_estimate0.8220
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.7
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.417
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha61010000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)