9mc6

Cryo-EM structure of Human UBA1-UBE2O-Ub -Transthiolation state 2

Method: ELECTRON MICROSCOPY Dmax: 113.8 Å Quality: GOOD

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

Ubiquitin-like modifier-activating enzyme 1

Homo sapiens

UniProt P22314

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 1–1058 Not recorded (E3-independent) E2 ubiquitin-conjugating enzyme × 1 (Q9C0C9) Ubiquitin × 1 (P0CG47) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBA1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1058; UniProt 1–1058

(E3-independent) E2 ubiquitin-conjugating enzyme

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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–1292 Not recorded Ubiquitin-like modifier-activating enzyme 1 × 1 (P22314) Ubiquitin × 1 (P0CG47) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1292; UniProt 1–1292

Ubiquitin

Homo sapiens

UniProt P0CG47

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 Ubiquitin-like modifier-activating enzyme 1 × 1 (P22314) (E3-independent) E2 ubiquitin-conjugating enzyme × 1 (Q9C0C9) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_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 9mc6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mc6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mc6
Deposition date deposition_date2025-03-17
Structure title titleCryo-EM structure of Human UBA1-UBE2O-Ub -Transthiolation state 2
Keywords keywordscryo-EM, UBA1, UBE2O, Ubiquitin, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.80
Radius of gyration Rg (electron density) rg_electron34.98
Forward intensity I(0) i0332300000.00
Molecular weight molecular_weight148040.0 kDa
Excluded volume excluded_volume185650 ų
Envelope volume envelope_volume245590 ų
Hydration-shell volume shell_volume57264 ų
Envelope diameter envelope_diameter122.6
Shell Rg shell_rg42.64
Envelope Rg envelope_rg34.52
Shape Rg shape_rg34.99
Total Rg total_rg35.50
Total atoms total_atoms10427
Residues n_residues1316
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 dmax113.8
Rg (real space) rg_real35.62
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real3.3230e+08
I(0) uncertainty (real space) i0_real_error6.0660e+06
Rg (reciprocal space) rg_reciprocal35.73
I(0) (reciprocal space) i0_reciprocal332300000.0000
Solution quality estimate total_estimate0.8912
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.5
Skewness Skewness skewness0.177
Kurtosis Kurtosis kurtosis-0.408
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55080000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.892

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)