7k6p

Active state Dot1 bound to the unacetylated H4 nucleosome

Method: ELECTRON MICROSCOPY Dmax: 124.7 Å Quality: EXCELLENT

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 Protein–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 38–135 Chain E; UniProt 38–135 Mutation:K79M, G103A Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (146-MER) × 1 DNA (146-MER) × 1 Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q04089) Ubiquitin × 1 (P0CG48) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

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 1–98; UniProt 38–135 Author chain E; PDBConstruct 1–98; UniProt 38–135

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 Protein–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 14–103 Chain F; UniProt 14–103 Not recorded Histone H3.2 × 2 (P84233) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (146-MER) × 1 DNA (146-MER) × 1 Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q04089) Ubiquitin × 1 (P0CG48) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 1–90; UniProt 14–103 Author chain F; PDBConstruct 1–90; UniProt 14–103

Histone H2A type 1

Xenopus laevis

UniProt P06897

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 13–119 Chain G; UniProt 13–119 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (146-MER) × 1 DNA (146-MER) × 1 Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q04089) Ubiquitin × 1 (P0CG48) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

136 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–107; UniProt 13–119 Author chain G; PDBConstruct 1–107; UniProt 13–119

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 Protein–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 33–125 Chain H; UniProt 33–125 Mutation:K120C,S32T Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) DNA (146-MER) × 1 DNA (146-MER) × 1 Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q04089) Ubiquitin × 1 (P0CG48) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 1–93; UniProt 33–125 Author chain H; PDBConstruct 1–93; UniProt 33–125

Histone-lysine N-methyltransferase, H3 lysine-79 specific

Saccharomyces cerevisiae

UniProt Q04089

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 176–580 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (146-MER) × 1 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DOT1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–405; UniProt 176–580

Ubiquitin

Homo sapiens

UniProt P0CG48

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain L; UniProt 1–76 Mutation:G76C Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (146-MER) × 1 DNA (146-MER) × 1 Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q04089) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

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

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 7k6p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7k6p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7k6p
Deposition date deposition_date2020-09-21
Structure title titleActive state Dot1 bound to the unacetylated H4 nucleosome
Keywords keywordsStructural Protein/DNA/Transferase, TRANSFERASE, Structural Protein-DNA-Transferase complex; Structural Protein/DNA/Transferase
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.91
Radius of gyration Rg (electron density) rg_electron40.12
Forward intensity I(0) i01198870000.00
Molecular weight molecular_weight224810.0 kDa
Excluded volume excluded_volume256120 ų
Envelope volume envelope_volume372420 ų
Hydration-shell volume shell_volume74315 ų
Envelope diameter envelope_diameter129.1
Shell Rg shell_rg48.03
Envelope Rg envelope_rg39.49
Shape Rg shape_rg40.03
Total Rg total_rg40.67
Total atoms total_atoms15447
Residues n_residues1511
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 dmax124.7
Rg (real space) rg_real41.64
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real1.1990e+09
I(0) uncertainty (real space) i0_real_error1.9870e+07
Rg (reciprocal space) rg_reciprocal41.91
I(0) (reciprocal space) i0_reciprocal1199000000.0000
Solution quality estimate total_estimate0.9001
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.8
Skewness Skewness skewness0.012
Kurtosis Kurtosis kurtosis-0.623
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha111200000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.955; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.862

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id7k6pA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7k6pD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7k6pE01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7k6pH01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7k6pL01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)