9egv

HOIL-1 RING2 domain bound to ubiquitin

Method: X-RAY DIFFRACTION Dmax: 75.7 Å Quality: GOOD

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

RanBP-type and C3HC4-type zinc finger-containing protein 1

Homo sapiens

UniProt Q9BYM8

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 425–510 Chain B; UniProt 425–510 Mutation:C460A Polyubiquitin-C × 1 (P0CG48) ZN ZINC ION × 6 CL CHLORIDE ION × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.2;293 K;0.01 M magnesium chloride hexahydrate, 0.05 M MES monohydrate pH 6.2, 1.8 M lithium sulfate monohydrate Resolution 2.00 Å R-free 0.208
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: dimeric(2) Count mismatch; review required Chain A; UniProt 425–510 Chain B; UniProt 425–510 Mutation:C460A Polyubiquitin-C × 1 (P0CG48) ZN ZINC ION × 6 CL CHLORIDE ION × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.2;293 K;0.01 M magnesium chloride hexahydrate, 0.05 M MES monohydrate pH 6.2, 1.8 M lithium sulfate monohydrate Resolution 2.00 Å R-free 0.208

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 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HOIL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–88; UniProt 425–510 Author chain B; PDBConstruct 3–88; UniProt 425–510

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 76–152 Not recorded RanBP-type and C3HC4-type zinc finger-containing protein 1 × 2 (Q9BYM8) ZN ZINC ION × 6 CL CHLORIDE ION × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.2;293 K;0.01 M magnesium chloride hexahydrate, 0.05 M MES monohydrate pH 6.2, 1.8 M lithium sulfate monohydrate Resolution 2.00 Å R-free 0.208
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: dimeric(2) Count mismatch; review required Chain C; UniProt 76–152 Not recorded RanBP-type and C3HC4-type zinc finger-containing protein 1 × 2 (Q9BYM8) ZN ZINC ION × 6 CL CHLORIDE ION × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.2;293 K;0.01 M magnesium chloride hexahydrate, 0.05 M MES monohydrate pH 6.2, 1.8 M lithium sulfate monohydrate Resolution 2.00 Å R-free 0.208

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 347 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 12–88; UniProt 76–152

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 9egv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9egv
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9egv
Deposition date deposition_date2024-11-21
Structure title titleHOIL-1 RING2 domain bound to ubiquitin
Keywords keywordsRBR E3 ubiquitin ligase, enzyme-substrate complex, RING2 domain, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.56
Radius of gyration Rg (electron density) rg_electron20.73
Forward intensity I(0) i016302300.00
Molecular weight molecular_weight27597.0 kDa
Excluded volume excluded_volume33344 ų
Envelope volume envelope_volume41590 ų
Hydration-shell volume shell_volume17711 ų
Envelope diameter envelope_diameter72.5
Shell Rg shell_rg26.34
Envelope Rg envelope_rg20.84
Shape Rg shape_rg20.72
Total Rg total_rg21.50
Total atoms total_atoms3721
Residues n_residues243
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 dmax75.7
Rg (real space) rg_real21.52
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.6300e+07
I(0) uncertainty (real space) i0_real_error2.3280e+05
Rg (reciprocal space) rg_reciprocal21.53
I(0) (reciprocal space) i0_reciprocal16300000.0000
Solution quality estimate total_estimate0.8728
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.7
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1778000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.894; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)