9m7o

Cryo-EM structure of Ufd2/Ubc4-ub complex with K29triUb(monomeric conformation)

Method: ELECTRON MICROSCOPY Dmax: 125.9 Å Quality: GOOD

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

Ubiquitin-conjugating enzyme E2 4

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P15731

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–148 Mutation:C22S/C102S Polyubiquitin-C × 1 (P0CG48) Polyubiquitin-C × 1 (P0CG48) Ubiquitin × 1 (P62979) E4 ubiquitin-protein ligase UFD2 × 1 (P54860) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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 UBC4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–148; UniProt 1–148

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–76 Chain E; UniProt 1–76 Mutation:K48C Mutation:K29R Ubiquitin-conjugating enzyme E2 4 × 1 (P15731) Ubiquitin × 1 (P62979) E4 ubiquitin-protein ligase UFD2 × 1 (P54860) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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 2, 3
Chains and sequence ranges Author chain D; PDBConstruct 1–76; UniProt 1–76 Author chain E; PDBConstruct 1–76; UniProt 1–76

Ubiquitin

Homo sapiens

UniProt P62979

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–76 Not recorded Ubiquitin-conjugating enzyme E2 4 × 1 (P15731) Polyubiquitin-C × 1 (P0CG48) Polyubiquitin-C × 1 (P0CG48) E4 ubiquitin-protein ligase UFD2 × 1 (P54860) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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.

221 other PDB entries and 235 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS27A_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–76; UniProt 1–76

E4 ubiquitin-protein ligase UFD2

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P54860

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–961 Not recorded Ubiquitin-conjugating enzyme E2 4 × 1 (P15731) Polyubiquitin-C × 1 (P0CG48) Polyubiquitin-C × 1 (P0CG48) Ubiquitin × 1 (P62979) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UFD2_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain A; PDBConstruct 1–961; UniProt 1–961

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 9m7o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m7o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m7o
Deposition date deposition_date2025-03-10
Structure title titleCryo-EM structure of Ufd2/Ubc4-ub complex with K29triUb(monomeric conformation)
Keywords keywordsE4 enzyme, Ufd2, branch Ub chains, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.73
Radius of gyration Rg (electron density) rg_electron36.10
Forward intensity I(0) i0252577000.00
Molecular weight molecular_weight131890.0 kDa
Excluded volume excluded_volume166770 ų
Envelope volume envelope_volume231970 ų
Hydration-shell volume shell_volume53871 ų
Envelope diameter envelope_diameter135.1
Shell Rg shell_rg42.38
Envelope Rg envelope_rg35.56
Shape Rg shape_rg36.09
Total Rg total_rg36.60
Total atoms total_atoms9310
Residues n_residues1179
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 dmax125.9
Rg (real space) rg_real36.69
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real2.5260e+08
I(0) uncertainty (real space) i0_real_error4.7160e+06
Rg (reciprocal space) rg_reciprocal36.72
I(0) (reciprocal space) i0_reciprocal252600000.0000
Solution quality estimate total_estimate0.8769
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.9
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.265
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48710000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)