7ea5

Yeast Set2 bound to a nucleosome containing oncohistone mutations

Method: ELECTRON MICROSCOPY Dmax: 147.3 Å Quality: GOOD

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

Histone H3

Xenopus laevis

UniProt A0A310TTQ1

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 35–135 Chain E; UniProt 35–135 Mutation:K37M Histone H4 × 2 Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) 601-DNA × 1 601-DNA × 1 Histone-lysine N-methyltransferase, H3 lysine-36 specific × 1 (A0A6V8RR65) ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

126 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A310TTQ1_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–101; UniProt 35–135 Author chain E; PDBConstruct 1–101; UniProt 35–135

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 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 14–118 Chain G; UniProt 14–118 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 Histone H2B × 2 (A0A1L8FQA5) 601-DNA × 1 601-DNA × 1 Histone-lysine N-methyltransferase, H3 lysine-36 specific × 1 (A0A6V8RR65) ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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 1–105; UniProt 14–118 Author chain G; PDBConstruct 1–105; UniProt 14–118

Histone H2B

Xenopus laevis

UniProt A0A1L8FQA5

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 32–124 Chain H; UniProt 32–124 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 Histone H2A × 2 (Q6AZJ8) 601-DNA × 1 601-DNA × 1 Histone-lysine N-methyltransferase, H3 lysine-36 specific × 1 (A0A6V8RR65) ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

6 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A1L8FQA5_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–93; UniProt 32–124 Author chain H; PDBConstruct 1–93; UniProt 32–124

Histone-lysine N-methyltransferase, H3 lysine-36 specific

Saccharomyces cerevisiae

UniProt A0A6V8RR65

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain K; UniProt 33–260 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) 601-DNA × 1 601-DNA × 1 ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6V8RR65_YEASX
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–228; UniProt 33–260

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 7ea5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ea5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ea5
Deposition date deposition_date2021-03-06
Structure title titleYeast Set2 bound to a nucleosome containing oncohistone mutations
Keywords keywordsmethyltransferase, Set2, nucleosome, H3K36M mutation, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.60
Radius of gyration Rg (electron density) rg_electron42.63
Forward intensity I(0) i01021240000.00
Molecular weight molecular_weight201340.0 kDa
Excluded volume excluded_volume226130 ų
Envelope volume envelope_volume363140 ų
Hydration-shell volume shell_volume70586 ų
Envelope diameter envelope_diameter148.3
Shell Rg shell_rg48.27
Envelope Rg envelope_rg42.11
Shape Rg shape_rg42.52
Total Rg total_rg43.10
Total atoms total_atoms13770
Residues n_residues1265
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 dmax147.3
Rg (real space) rg_real44.51
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real1.0210e+09
I(0) uncertainty (real space) i0_real_error1.9830e+07
Rg (reciprocal space) rg_reciprocal44.60
I(0) (reciprocal space) i0_reciprocal1021000000.0000
Solution quality estimate total_estimate0.8860
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.5
Skewness Skewness skewness0.260
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha96950000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id7ea5A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5D01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5E01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5F01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5H01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)