7xcr

Cryo-EM structure of Dot1L and H2BK34ub-H3K79Nle nucleosome 1:1 complex

Method: ELECTRON MICROSCOPY Dmax: 133.1 Å Quality: GOOD

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

Ubiquitin

Homo sapiens

UniProt P0CG47

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 Not recorded Histone H4 × 2 (A0A672GII6) Histone H2A × 2 (Q08AJ9) Histone H2B type 1-K × 2 (O60814) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) Histone domain-containing protein × 2 (S4RAZ3) DNA (146-MER) × 1 DNA (146-MER) × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

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

Histone H4

Homo sapiens

UniProt A0A672GII6

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 6–93 Chain F; UniProt 6–93 Not recorded Ubiquitin × 1 (P0CG47) Histone H2A × 2 (Q08AJ9) Histone H2B type 1-K × 2 (O60814) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) Histone domain-containing protein × 2 (S4RAZ3) DNA (146-MER) × 1 DNA (146-MER) × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 A0A672GII6_SALFA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–88; UniProt 6–93 Author chain F; PDBConstruct 1–88; UniProt 6–93

Histone H2A

Homo sapiens

UniProt Q08AJ9

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 12–119 Chain G; UniProt 12–119 Not recorded Ubiquitin × 1 (P0CG47) Histone H4 × 2 (A0A672GII6) Histone H2B type 1-K × 2 (O60814) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) Histone domain-containing protein × 2 (S4RAZ3) DNA (146-MER) × 1 DNA (146-MER) × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q08AJ9_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–108; UniProt 12–119 Author chain G; PDBConstruct 1–108; UniProt 12–119

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 32–125 Chain H; UniProt 32–125 Not recorded Ubiquitin × 1 (P0CG47) Histone H4 × 2 (A0A672GII6) Histone H2A × 2 (Q08AJ9) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) Histone domain-containing protein × 2 (S4RAZ3) DNA (146-MER) × 1 DNA (146-MER) × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 1–94; UniProt 32–125 Author chain H; PDBConstruct 1–94; UniProt 32–125

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 5–332 Not recorded Ubiquitin × 1 (P0CG47) Histone H4 × 2 (A0A672GII6) Histone H2A × 2 (Q08AJ9) Histone H2B type 1-K × 2 (O60814) Histone domain-containing protein × 2 (S4RAZ3) DNA (146-MER) × 1 DNA (146-MER) × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 5
Chains and sequence ranges Author chain K; PDBConstruct 1–328; UniProt 5–332

Histone domain-containing protein

OrganismNot specified

UniProt S4RAZ3

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 61–159 Chain E; UniProt 61–159 Non-standard monomer:Yes (specific site not provided by mmCIF) Ubiquitin × 1 (P0CG47) Histone H4 × 2 (A0A672GII6) Histone H2A × 2 (Q08AJ9) Histone H2B type 1-K × 2 (O60814) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) DNA (146-MER) × 1 DNA (146-MER) × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S4RAZ3_PETMA
Isoform
PDB entities 6
Chains and sequence ranges Author chain A; PDBConstruct 1–99; UniProt 61–159 Author chain E; PDBConstruct 1–99; UniProt 61–159

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 7xcr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7xcr
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7xcr
Deposition date deposition_date2022-03-25
Structure title titleCryo-EM structure of Dot1L and H2BK34ub-H3K79Nle nucleosome 1:1 complex
Keywords keywordsComplex, Dot1L, H2BK34ub, Nucleosome, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.93
Radius of gyration Rg (electron density) rg_electron41.20
Forward intensity I(0) i01194090000.00
Molecular weight molecular_weight224170.0 kDa
Excluded volume excluded_volume255470 ų
Envelope volume envelope_volume385750 ų
Hydration-shell volume shell_volume75711 ų
Envelope diameter envelope_diameter137.7
Shell Rg shell_rg48.30
Envelope Rg envelope_rg40.70
Shape Rg shape_rg41.10
Total Rg total_rg41.73
Total atoms total_atoms15400
Residues n_residues1464
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 dmax133.1
Rg (real space) rg_real42.67
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real1.1940e+09
I(0) uncertainty (real space) i0_real_error2.0260e+07
Rg (reciprocal space) rg_reciprocal42.93
I(0) (reciprocal space) i0_reciprocal1194000000.0000
Solution quality estimate total_estimate0.8916
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.6
Skewness Skewness skewness0.057
Kurtosis Kurtosis kurtosis-0.553
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha92690000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.866

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7xcrD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7xcrH01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7xcrL01
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)