6nzo

Set2 bound to nucleosome

Method: ELECTRON MICROSCOPY Dmax: 137.5 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 Insufficient information Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Mutation:K36M Histone H4 × 2 (P62799) Ubiquitin-60S ribosomal protein L40,Histone H2A × 2 (P0CH09,Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3 × 2 (A0A310TTQ1) Ubiquitin-60S ribosomal protein L40,Histone H2A × 2 (P0CH09,Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

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 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Ubiquitin-60S ribosomal protein L40,Histone H2A

Xenopus laevis

UniProt P0CH09

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 1–75 Chain G; UniProt 1–75 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 RL40B_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 21–95; UniProt 1–75 Author chain G; PDBConstruct 21–95; UniProt 1–75

Ubiquitin-60S ribosomal protein L40,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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 18–130 Chain G; UniProt 18–130 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 109–221; UniProt 18–130 Author chain G; PDBConstruct 109–221; UniProt 18–130

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Mutation:S29T Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Ubiquitin-60S ribosomal protein L40,Histone H2A × 2 (P0CH09,Q6AZJ8) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

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 2–123; UniProt 5–126 Author chain H; PDBConstruct 2–123; UniProt 5–126

Histone-lysine N-methyltransferase

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

UniProt G0S676

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain S; UniProt 1–939 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Ubiquitin-60S ribosomal protein L40,Histone H2A × 2 (P0CH09,Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S676_CHATD
Isoform
PDB entities 7
Chains and sequence ranges Author chain S; PDBConstruct 1–939; UniProt 1–939

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 6nzo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6nzo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6nzo
Deposition date deposition_date2019-02-14
Structure title titleSet2 bound to nucleosome
Keywords keywordsSet2, nucleosome, chromatin, KMT, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.02
Radius of gyration Rg (electron density) rg_electron41.11
Forward intensity I(0) i01024360000.00
Molecular weight molecular_weight200900.0 kDa
Excluded volume excluded_volume225330 ų
Envelope volume envelope_volume340740 ų
Hydration-shell volume shell_volume68290 ų
Envelope diameter envelope_diameter140.6
Shell Rg shell_rg47.23
Envelope Rg envelope_rg40.70
Shape Rg shape_rg41.00
Total Rg total_rg41.61
Total atoms total_atoms13738
Residues n_residues1275
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 dmax137.5
Rg (real space) rg_real42.93
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real1.0240e+09
I(0) uncertainty (real space) i0_real_error2.0100e+07
Rg (reciprocal space) rg_reciprocal43.02
I(0) (reciprocal space) i0_reciprocal1024000000.0000
Solution quality estimate total_estimate0.8855
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.3
Skewness Skewness skewness0.245
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha100700000.0000
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: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.761

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6nzoA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoH00
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)