4r8p

Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle

Method: X-RAY DIFFRACTION Dmax: 127.1 Å Quality: REASONABLE

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

Histone H3.2

Xenopus laevis

UniProt P84233

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 Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-mer) × 1 DNA (147-mer) × 1 Polycomb complex protein BMI-1 × 2 (P35226) E3 ubiquitin-protein ligase RING2, Ubiquitin-conjugating enzyme E2 D3 × 2 (Q99496,P61077) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:Modified micro batch under oil;pH 7.5;294 K;25 mM HEPES pH 7.5, 80 mM NH4NO3, 3 % PEG2000-MME, Modified micro batch under oil, temperature 294K Resolution 3.28 Å R-free 0.245

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.

230 other PDB entries and 239 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

Histone H4

Xenopus laevis

UniProt P62799

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 Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded Histone H3.2 × 2 (P84233) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-mer) × 1 DNA (147-mer) × 1 Polycomb complex protein BMI-1 × 2 (P35226) E3 ubiquitin-protein ligase RING2, Ubiquitin-conjugating enzyme E2 D3 × 2 (Q99496,P61077) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:Modified micro batch under oil;pH 7.5;294 K;25 mM HEPES pH 7.5, 80 mM NH4NO3, 3 % PEG2000-MME, Modified micro batch under oil, temperature 294K Resolution 3.28 Å R-free 0.245

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.

354 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

Histone H2A

Xenopus laevis

UniProt Q6AZJ8

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 Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (147-mer) × 1 DNA (147-mer) × 1 Polycomb complex protein BMI-1 × 2 (P35226) E3 ubiquitin-protein ligase RING2, Ubiquitin-conjugating enzyme E2 D3 × 2 (Q99496,P61077) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:Modified micro batch under oil;pH 7.5;294 K;25 mM HEPES pH 7.5, 80 mM NH4NO3, 3 % PEG2000-MME, Modified micro batch under oil, temperature 294K Resolution 3.28 Å R-free 0.245

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.

226 other PDB entries and 238 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6AZJ8_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

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 Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) DNA (147-mer) × 1 DNA (147-mer) × 1 Polycomb complex protein BMI-1 × 2 (P35226) E3 ubiquitin-protein ligase RING2, Ubiquitin-conjugating enzyme E2 D3 × 2 (Q99496,P61077) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:Modified micro batch under oil;pH 7.5;294 K;25 mM HEPES pH 7.5, 80 mM NH4NO3, 3 % PEG2000-MME, Modified micro batch under oil, temperature 294K Resolution 3.28 Å R-free 0.245

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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–122; UniProt 5–126 Author chain H; PDBConstruct 1–122; UniProt 5–126

Polycomb complex protein BMI-1

Homo sapiens

UniProt P35226

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 Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain K; UniProt 2–109 Chain M; UniProt 2–109 Fragment:Residues 2-109 Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-mer) × 1 DNA (147-mer) × 1 E3 ubiquitin-protein ligase RING2, Ubiquitin-conjugating enzyme E2 D3 × 2 (Q99496,P61077) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:Modified micro batch under oil;pH 7.5;294 K;25 mM HEPES pH 7.5, 80 mM NH4NO3, 3 % PEG2000-MME, Modified micro batch under oil, temperature 294K Resolution 3.28 Å R-free 0.245

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.

21 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BMI1_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 3–110; UniProt 2–109 Author chain M; PDBConstruct 3–110; UniProt 2–109

E3 ubiquitin-protein ligase RING2, Ubiquitin-conjugating enzyme E2 D3

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 Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain L; UniProt 2–147 Chain N; UniProt 2–147 Fragment:Residues 2-116 of Ring1B and Residues 2-148 of UbcH5c Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-mer) × 1 DNA (147-mer) × 1 Polycomb complex protein BMI-1 × 2 (P35226) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:Modified micro batch under oil;pH 7.5;294 K;25 mM HEPES pH 7.5, 80 mM NH4NO3, 3 % PEG2000-MME, Modified micro batch under oil, temperature 294K Resolution 3.28 Å R-free 0.245

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 8
Chains and sequence ranges Author chain L; PDBConstruct 123–268; UniProt 2–147 Author chain N; PDBConstruct 123–268; UniProt 2–147

E3 ubiquitin-protein ligase RING2, Ubiquitin-conjugating enzyme E2 D3

Homo sapiens

UniProt Q99496

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 Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain L; UniProt 2–116 Chain N; UniProt 2–116 Fragment:Residues 2-116 of Ring1B and Residues 2-148 of UbcH5c Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-mer) × 1 DNA (147-mer) × 1 Polycomb complex protein BMI-1 × 2 (P35226) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:Modified micro batch under oil;pH 7.5;294 K;25 mM HEPES pH 7.5, 80 mM NH4NO3, 3 % PEG2000-MME, Modified micro batch under oil, temperature 294K Resolution 3.28 Å R-free 0.245

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.

24 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RING2_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 2–116; UniProt 2–116 Author chain N; PDBConstruct 2–116; UniProt 2–116

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 4r8p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4r8p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4r8p
Deposition date deposition_date2014-09-02
Structure title titleCrystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle
Keywords keywordsRING domain, Arginine anchor, Ubiquitin ligase, Histone modification enzyme, Structural Protein-DNA complex; Structural Protein/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.37
Radius of gyration Rg (electron density) rg_electron40.80
Forward intensity I(0) i01421330000.00
Molecular weight molecular_weight249420.0 kDa
Excluded volume excluded_volume286240 ų
Envelope volume envelope_volume428950 ų
Hydration-shell volume shell_volume83440 ų
Envelope diameter envelope_diameter139.3
Shell Rg shell_rg49.56
Envelope Rg envelope_rg40.07
Shape Rg shape_rg40.74
Total Rg total_rg41.28
Total atoms total_atoms17134
Residues n_residues1762
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 dmax127.1
Rg (real space) rg_real42.04
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.4210e+09
I(0) uncertainty (real space) i0_real_error2.4910e+07
Rg (reciprocal space) rg_reciprocal42.37
I(0) (reciprocal space) i0_reciprocal1422000000.0000
Solution quality estimate total_estimate0.6841
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.0
Skewness Skewness skewness-0.017
Kurtosis Kurtosis kurtosis-0.565
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118600000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 0.083; Positv: 1.000; Valcen: 0.945; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id4r8pA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4r8pB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4r8pC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4r8pD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4r8pE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4r8pF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4r8pG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4r8pH00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4r8pK00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id4r8pL01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id4r8pM00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id4r8pN01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)

8. Citations (1)

9. Files and Curves (10)