9d1i

Structure of Ubiquitin bound to KLHDC3-EloB/C

Method: X-RAY DIFFRACTION Dmax: 112.0 Å Quality: GOOD

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

Kelch domain-containing protein 3

Homo sapiens

UniProt Q9BQ90

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 1–382 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Ubiquitin × 1 (P0CG47) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;10%PEG5KMME, 0.1M HEPES pH=7.0, 5% Tascsimate pH=7.0 Resolution 2.00 Å R-free 0.189

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 KLDC3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–383; UniProt 1–382

Elongin-B

Homo sapiens

UniProt Q15370

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 1–104 Not recorded Kelch domain-containing protein 3 × 1 (Q9BQ90) Elongin-C × 1 (Q15369) Ubiquitin × 1 (P0CG47) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;10%PEG5KMME, 0.1M HEPES pH=7.0, 5% Tascsimate pH=7.0 Resolution 2.00 Å R-free 0.189

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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–104; UniProt 1–104

Elongin-C

Homo sapiens

UniProt Q15369

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 C; UniProt 16–112 Not recorded Kelch domain-containing protein 3 × 1 (Q9BQ90) Elongin-B × 1 (Q15370) Ubiquitin × 1 (P0CG47) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;10%PEG5KMME, 0.1M HEPES pH=7.0, 5% Tascsimate pH=7.0 Resolution 2.00 Å R-free 0.189

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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 25–121; UniProt 16–112

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–76 Not recorded Kelch domain-containing protein 3 × 1 (Q9BQ90) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;10%PEG5KMME, 0.1M HEPES pH=7.0, 5% Tascsimate pH=7.0 Resolution 2.00 Å R-free 0.189

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 4
Chains and sequence ranges Author chain D; 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 9d1i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9d1i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9d1i
Deposition date deposition_date2024-08-07
Structure title titleStructure of Ubiquitin bound to KLHDC3-EloB/C
Keywords keywordsKLHDC3, Ubiquitin, C-degron, Cullin-RING, E3, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.78
Radius of gyration Rg (electron density) rg_electron30.43
Forward intensity I(0) i079160600.00
Molecular weight molecular_weight69731.0 kDa
Excluded volume excluded_volume86978 ų
Envelope volume envelope_volume108290 ų
Hydration-shell volume shell_volume31476 ų
Envelope diameter envelope_diameter119.2
Shell Rg shell_rg35.28
Envelope Rg envelope_rg30.73
Shape Rg shape_rg30.43
Total Rg total_rg30.86
Total atoms total_atoms4911
Residues n_residues631
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 dmax112.0
Rg (real space) rg_real31.06
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real7.9160e+07
I(0) uncertainty (real space) i0_real_error1.4460e+06
Rg (reciprocal space) rg_reciprocal30.94
I(0) (reciprocal space) i0_reciprocal79150000.0000
Solution quality estimate total_estimate0.8033
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.564
Kurtosis Kurtosis kurtosis-0.199
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22900000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.627; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.568; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)