6jm9

cryo-EM structure of DOT1L bound to unmodified nucleosome

Method: ELECTRON MICROSCOPY Dmax: 123.2 Å Quality: GOOD

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 39–136 Chain E; UniProt 39–136 Not recorded DNA strand I × 1 DNA strand J × 1 Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.30 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.

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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–98; UniProt 39–136 Author chain E; PDBConstruct 1–98; UniProt 39–136

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 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain B; UniProt 17–103 Chain F; UniProt 17–103 Not recorded DNA strand I × 1 DNA strand J × 1 Histone H3.2 × 2 (P84233) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.30 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.

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 4
Chains and sequence ranges Author chain B; PDBConstruct 1–87; UniProt 17–103 Author chain F; PDBConstruct 1–87; UniProt 17–103

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 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 15–121 Chain G; UniProt 15–121 Not recorded DNA strand I × 1 DNA strand J × 1 Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.30 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 5
Chains and sequence ranges Author chain C; PDBConstruct 1–107; UniProt 15–121 Author chain G; PDBConstruct 1–107; UniProt 15–121

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 34–126 Chain H; UniProt 34–126 Not recorded DNA strand I × 1 DNA strand J × 1 Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.30 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.

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 6
Chains and sequence ranges Author chain D; PDBConstruct 2–94; UniProt 34–126 Author chain H; PDBConstruct 2–94; UniProt 34–126

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

Homo sapiens

UniProt Q8TEK3

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 X; UniProt 5–332 Not recorded DNA strand I × 1 DNA strand J × 1 Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.30 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.

47 other PDB entries and 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DOT1L_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain X; PDBConstruct 1–328; UniProt 5–332

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 6jm9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6jm9
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6jm9
Deposition date deposition_date2019-03-07
Structure title titlecryo-EM structure of DOT1L bound to unmodified nucleosome
Keywords keywordshistone, nucleosome, methylation, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.11
Radius of gyration Rg (electron density) rg_electron38.27
Forward intensity I(0) i0935688000.00
Molecular weight molecular_weight200940.0 kDa
Excluded volume excluded_volume230780 ų
Envelope volume envelope_volume334100 ų
Hydration-shell volume shell_volume70128 ų
Envelope diameter envelope_diameter128.1
Shell Rg shell_rg46.35
Envelope Rg envelope_rg37.67
Shape Rg shape_rg38.16
Total Rg total_rg38.89
Total atoms total_atoms13827
Residues n_residues1340
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 dmax123.2
Rg (real space) rg_real39.88
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real9.3570e+08
I(0) uncertainty (real space) i0_real_error1.6450e+07
Rg (reciprocal space) rg_reciprocal40.11
I(0) (reciprocal space) i0_reciprocal935900000.0000
Solution quality estimate total_estimate0.8984
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.7
Skewness Skewness skewness0.041
Kurtosis Kurtosis kurtosis-0.567
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha58560000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)