9u5u

The 1:1 cryo-EM structure of BAP1/ASXL1-K351Ub in complex with H2AK119Ub nucleosome

Method: ELECTRON MICROSCOPY Dmax: 129.8 Å Quality: REASONABLE

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

Histone H3.2

Homo sapiens

UniProt Q71DI3

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–DNA 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 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 Ubiquitin carboxyl-terminal hydrolase BAP1 × 1 (Q92560) Ubiquitin × 2 (P62979) Polycomb group protein ASXL1 × 1 (Q8IXJ9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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.

139 other PDB entries and 157 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_HUMAN
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

Homo sapiens

UniProt P62805

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–DNA 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 (Q71DI3) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 Ubiquitin carboxyl-terminal hydrolase BAP1 × 1 (Q92560) Ubiquitin × 2 (P62979) Polycomb group protein ASXL1 × 1 (Q8IXJ9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
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 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 Protein–DNA 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 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B type 1-K × 2 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 Ubiquitin carboxyl-terminal hydrolase BAP1 × 1 (Q92560) Ubiquitin × 2 (P62979) Polycomb group protein ASXL1 × 1 (Q8IXJ9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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.

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 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 type 1-K

Homo sapiens

UniProt O60814

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain D; UniProt 2–126 Chain H; UniProt 2–126 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) DNA (147-MER) × 1 DNA (147-MER) × 1 Ubiquitin carboxyl-terminal hydrolase BAP1 × 1 (Q92560) Ubiquitin × 2 (P62979) Polycomb group protein ASXL1 × 1 (Q8IXJ9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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.

82 other PDB entries and 82 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1K_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

Ubiquitin carboxyl-terminal hydrolase BAP1

Homo sapiens

UniProt Q92560

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain L; UniProt 5–715 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 Ubiquitin × 2 (P62979) Polycomb group protein ASXL1 × 1 (Q8IXJ9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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 BAP1_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain L; PDBConstruct 1–711; UniProt 5–715

Ubiquitin

Homo sapiens

UniProt P62979

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain M; UniProt 1–76 Chain O; UniProt 1–76 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 Ubiquitin carboxyl-terminal hydrolase BAP1 × 1 (Q92560) Polycomb group protein ASXL1 × 1 (Q8IXJ9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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.

221 other PDB entries and 235 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS27A_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain M; PDBConstruct 1–76; UniProt 1–76 Author chain O; PDBConstruct 1–76; UniProt 1–76

Polycomb group protein ASXL1

Homo sapiens

UniProt Q8IXJ9

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain N; UniProt 238–390 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) DNA (147-MER) × 1 DNA (147-MER) × 1 Ubiquitin carboxyl-terminal hydrolase BAP1 × 1 (Q92560) Ubiquitin × 2 (P62979) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASXL1_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain N; PDBConstruct 1–153; UniProt 238–390

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 9u5u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9u5u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9u5u
Deposition date deposition_date2025-03-21
Structure title titleThe 1:1 cryo-EM structure of BAP1/ASXL1-K351Ub in complex with H2AK119Ub nucleosome
Keywords keywords;PR-DUB, nucleosome, H2AK119Ub, BAP1, BAP1/ASXL1, ASXL1 K351Ub The 2:1 complex of BAP1-ASXL1-K351Ub and H2AK119Ub nucleosome, NUCLEAR PROTEIN/DNA, NUCLEAR PROTEIN-DNA complex ;; NUCLEAR PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.81
Radius of gyration Rg (electron density) rg_electron42.08
Forward intensity I(0) i01321920000.00
Molecular weight molecular_weight238260.0 kDa
Excluded volume excluded_volume272700 ų
Envelope volume envelope_volume427950 ų
Hydration-shell volume shell_volume82332 ų
Envelope diameter envelope_diameter139.4
Shell Rg shell_rg49.81
Envelope Rg envelope_rg40.75
Shape Rg shape_rg41.98
Total Rg total_rg42.61
Total atoms total_atoms16392
Residues n_residues1589
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 dmax129.8
Rg (real space) rg_real43.49
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.3220e+09
I(0) uncertainty (real space) i0_real_error2.0370e+07
Rg (reciprocal space) rg_reciprocal43.81
I(0) (reciprocal space) i0_reciprocal1322000000.0000
Solution quality estimate total_estimate0.6718
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.7
Skewness Skewness skewness0.006
Kurtosis Kurtosis kurtosis-0.577
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha105800000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 0.032; Positv: 1.000; Valcen: 0.954; Smooth: 0.839

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)