8c07

Structure of HECT E3 UBR5 forming K48 linked Ubiquitin chains

Method: ELECTRON MICROSCOPY Dmax: 103.5 Å Quality: REASONABLE

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

E3 ubiquitin-protein ligase UBR5

Homo sapiens

UniProt O95071

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 1–2799 Chain J; UniProt 1–2799 Not recorded Polyubiquitin-B × 1 (P0CG47) Polyubiquitin-B × 1 (P0CG47) SY8 5-azanylpentan-2-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBR5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 8–2806; UniProt 1–2799 Author chain J; PDBConstruct 8–2806; UniProt 1–2799

Polyubiquitin-B

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 1–76 Chain K; UniProt 1–76 Not recorded E3 ubiquitin-protein ligase UBR5 × 2 (O95071) SY8 5-azanylpentan-2-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 2, 3
Chains and sequence ranges Author chain I; PDBConstruct 1–76; UniProt 1–76 Author chain K; 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 8c07

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8c07
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8c07
Deposition date deposition_date2022-12-16
Structure title titleStructure of HECT E3 UBR5 forming K48 linked Ubiquitin chains
Keywords keywordsE3 ligase, UBR5, Ubiquitination, UBQ, Ubiquitin, HECT, K48, UBQ-chain, polyubiquitylation, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.45
Radius of gyration Rg (electron density) rg_electron29.79
Forward intensity I(0) i080160900.00
Molecular weight molecular_weight70567.0 kDa
Excluded volume excluded_volume88625 ų
Envelope volume envelope_volume121970 ų
Hydration-shell volume shell_volume35134 ų
Envelope diameter envelope_diameter106.6
Shell Rg shell_rg35.95
Envelope Rg envelope_rg29.90
Shape Rg shape_rg29.80
Total Rg total_rg30.40
Total atoms total_atoms4974
Residues n_residues644
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 dmax103.5
Rg (real space) rg_real30.53
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real8.0160e+07
I(0) uncertainty (real space) i0_real_error1.1490e+06
Rg (reciprocal space) rg_reciprocal30.50
I(0) (reciprocal space) i0_reciprocal80160000.0000
Solution quality estimate total_estimate0.6811
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.452
Kurtosis Kurtosis kurtosis-0.203
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28750000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.814; Stabil: 1.000; Sysdev: 0.193; Positv: 1.000; Valcen: 0.954; Smooth: 0.874

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8c07I01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id8c07K01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)