9gkm

Structure of HECT E3 TRIP12 forming K29/K48-branched Ubiquitin chains

Method: ELECTRON MICROSCOPY Dmax: 131.4 Å Quality: REASONABLE

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

Ubiquitin

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–75 Chain C; UniProt 1–76 Mutation:K29C Polyubiquitin-B × 1 (P0CG47) Isoform 3 of E3 ubiquitin-protein ligase TRIP12 × 1 (Q14669) SY8 5-azanylpentan-2-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.69 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 1, 2
Chains and sequence ranges Author chain B; PDBConstruct 1–75; UniProt 1–75 Author chain C; PDBConstruct 1–76; UniProt 1–76

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 D; UniProt 1–76 Mutation:K48R Ubiquitin × 1 (P0CG48) Polyubiquitin-C × 1 (P0CG48) Isoform 3 of E3 ubiquitin-protein ligase TRIP12 × 1 (Q14669) SY8 5-azanylpentan-2-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.69 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 D; PDBConstruct 1–76; UniProt 1–76

Isoform 3 of E3 ubiquitin-protein ligase TRIP12

Homo sapiens

UniProt Q14669

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 A; UniProt 478–2040 Not recorded Ubiquitin × 1 (P0CG48) Polyubiquitin-C × 1 (P0CG48) Polyubiquitin-B × 1 (P0CG47) SY8 5-azanylpentan-2-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.69 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRIPC_HUMAN
Isoform Q14669-3
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 3–1565; UniProt 478–2040

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 9gkm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9gkm
Deposition date deposition_date2024-08-25
Structure title titleStructure of HECT E3 TRIP12 forming K29/K48-branched Ubiquitin chains
Keywords keywordsLIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.72
Radius of gyration Rg (electron density) rg_electron40.06
Forward intensity I(0) i0364948000.00
Molecular weight molecular_weight159680.0 kDa
Excluded volume excluded_volume201800 ų
Envelope volume envelope_volume293940 ų
Hydration-shell volume shell_volume61067 ų
Envelope diameter envelope_diameter143.0
Shell Rg shell_rg45.89
Envelope Rg envelope_rg39.23
Shape Rg shape_rg40.06
Total Rg total_rg40.42
Total atoms total_atoms11231
Residues n_residues1446
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 dmax131.4
Rg (real space) rg_real40.62
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real3.6490e+08
I(0) uncertainty (real space) i0_real_error6.7010e+06
Rg (reciprocal space) rg_reciprocal40.72
I(0) (reciprocal space) i0_reciprocal365000000.0000
Solution quality estimate total_estimate0.6661
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.5
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis-0.357
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50110000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 1.000; Smooth: 0.867

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)