8uqa

Crystal structure of RNF168 (RING)-UbcH5c fused to H2A-H2B via a 12-residue linker

Method: X-RAY DIFFRACTION Dmax: 89.5 Å Quality: EXCELLENT

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

E3 ubiquitin-protein ligase RNF168,Ubiquitin-conjugating enzyme E2 D3,Histone H2B type 2-E,Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain K; UniProt 13–106 Mutation:C85K in UbcH5c NA SODIUM ION × 3 ZN ZINC ION × 2 CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;288 K;Crystals were obtained by mixing 2 microliters of the protein fusion (8.0 mg/mL) in 10 mM HEPES, pH 7.5, 600 mM NaCl, 1 mM TCEP and 2 microliters of the reservoir solution containing 0.1 M HEPES, pH 7.5, 2.4 M NaCl Resolution 2.05 Å R-free 0.231

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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 354–447; UniProt 13–106

E3 ubiquitin-protein ligase RNF168,Ubiquitin-conjugating enzyme E2 D3,Histone H2B type 2-E,Histone H2A type 1-B/E

Homo sapiens

UniProt P61077

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain K; UniProt 2–147 Mutation:C85K in UbcH5c NA SODIUM ION × 3 ZN ZINC ION × 2 CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;288 K;Crystals were obtained by mixing 2 microliters of the protein fusion (8.0 mg/mL) in 10 mM HEPES, pH 7.5, 600 mM NaCl, 1 mM TCEP and 2 microliters of the reservoir solution containing 0.1 M HEPES, pH 7.5, 2.4 M NaCl Resolution 2.05 Å R-free 0.231

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.

45 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2D3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 104–249; UniProt 2–147

E3 ubiquitin-protein ligase RNF168,Ubiquitin-conjugating enzyme E2 D3,Histone H2B type 2-E,Histone H2A type 1-B/E

Homo sapiens

UniProt Q16778

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain K; UniProt 34–124 Mutation:C85K in UbcH5c NA SODIUM ION × 3 ZN ZINC ION × 2 CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;288 K;Crystals were obtained by mixing 2 microliters of the protein fusion (8.0 mg/mL) in 10 mM HEPES, pH 7.5, 600 mM NaCl, 1 mM TCEP and 2 microliters of the reservoir solution containing 0.1 M HEPES, pH 7.5, 2.4 M NaCl Resolution 2.05 Å R-free 0.231

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.

39 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B2E_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 262–352; UniProt 34–124

E3 ubiquitin-protein ligase RNF168,Ubiquitin-conjugating enzyme E2 D3,Histone H2B type 2-E,Histone H2A type 1-B/E

Homo sapiens

UniProt Q8IYW5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain K; UniProt 1–94 Mutation:C85K in UbcH5c NA SODIUM ION × 3 ZN ZINC ION × 2 CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;288 K;Crystals were obtained by mixing 2 microliters of the protein fusion (8.0 mg/mL) in 10 mM HEPES, pH 7.5, 600 mM NaCl, 1 mM TCEP and 2 microliters of the reservoir solution containing 0.1 M HEPES, pH 7.5, 2.4 M NaCl Resolution 2.05 Å R-free 0.231

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.

38 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RN168_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 3–96; UniProt 1–94

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 8uqa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uqa
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8uqa
Deposition date deposition_date2023-10-23
Structure title titleCrystal structure of RNF168 (RING)-UbcH5c fused to H2A-H2B via a 12-residue linker
Keywords keywords;RNF168, UbcH5c, Histone H2A, Histone H2B, Chromatin, Ubiquitin ligase, Ubiquitin-conjugating enzyme, DNA damage response, DNA double-strand break repair, PROTEIN BINDING, PROTEIN BINDING-Transferase complex, TRANSFERASE ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.01
Radius of gyration Rg (electron density) rg_electron27.22
Forward intensity I(0) i039371500.00
Molecular weight molecular_weight47907.0 kDa
Excluded volume excluded_volume59795 ų
Envelope volume envelope_volume76495 ų
Hydration-shell volume shell_volume24758 ų
Envelope diameter envelope_diameter95.1
Shell Rg shell_rg32.92
Envelope Rg envelope_rg27.14
Shape Rg shape_rg27.19
Total Rg total_rg27.95
Total atoms total_atoms3349
Residues n_residues427
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 dmax89.5
Rg (real space) rg_real28.05
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real3.9370e+07
I(0) uncertainty (real space) i0_real_error6.1180e+05
Rg (reciprocal space) rg_reciprocal28.04
I(0) (reciprocal space) i0_reciprocal39370000.0000
Solution quality estimate total_estimate0.9011
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.7
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.678
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6342000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)