6nqa

Active state Dot1L bound to the H2B-Ubiquitinated nucleosome, 1-to-1 complex

Method: ELECTRON MICROSCOPY Dmax: 129.2 Å Quality: GOOD

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

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 2–103 Chain F; UniProt 2–103 Not recorded 601 DNA Strand 1 × 1 601 DNA Strand 2 × 1 Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) Ubiquitin × 1 (P0CG48) Histone H3.2 × 2 (P84233) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Solutions were prepared on the day of freezing and filtered though a 0.2 um filter prior to use. cryo-EM vitrification conditions:Cryogen ETHANE;Blot once for 3.5 seconds before freezing. Resolution 3.54 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 3
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

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 2–130 Chain G; UniProt 2–130 Mutation:G99R, A123S 601 DNA Strand 1 × 1 601 DNA Strand 2 × 1 Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) Ubiquitin × 1 (P0CG48) Histone H3.2 × 2 (P84233) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Solutions were prepared on the day of freezing and filtered though a 0.2 um filter prior to use. cryo-EM vitrification conditions:Cryogen ETHANE;Blot once for 3.5 seconds before freezing. Resolution 3.54 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 4
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

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 Protein–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Mutation:S32T, K120C 601 DNA Strand 1 × 1 601 DNA Strand 2 × 1 Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) Ubiquitin × 1 (P0CG48) Histone H3.2 × 2 (P84233) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Solutions were prepared on the day of freezing and filtered though a 0.2 um filter prior to use. cryo-EM vitrification conditions:Cryogen ETHANE;Blot once for 3.5 seconds before freezing. Resolution 3.54 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 5
Chains and sequence ranges Author chain D; PDBConstruct 1–122; UniProt 5–126 Author chain H; PDBConstruct 1–122; UniProt 5–126

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 2–416 Not recorded 601 DNA Strand 1 × 1 601 DNA Strand 2 × 1 Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Ubiquitin × 1 (P0CG48) Histone H3.2 × 2 (P84233) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Solutions were prepared on the day of freezing and filtered though a 0.2 um filter prior to use. cryo-EM vitrification conditions:Cryogen ETHANE;Blot once for 3.5 seconds before freezing. Resolution 3.54 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 6
Chains and sequence ranges Author chain K; PDBConstruct 2–416; UniProt 2–416

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 601 DNA Strand 1 × 1 601 DNA Strand 2 × 1 Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) Histone H3.2 × 2 (P84233) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Solutions were prepared on the day of freezing and filtered though a 0.2 um filter prior to use. cryo-EM vitrification conditions:Cryogen ETHANE;Blot once for 3.5 seconds before freezing. Resolution 3.54 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 7
Chains and sequence ranges Author chain L; PDBConstruct 5–80; UniProt 1–76

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 2–136 Chain E; UniProt 2–136 Mutation:G102A, K79Nle, M90Nle, M120Nle Non-standard monomer:Yes (specific site not provided by mmCIF) 601 DNA Strand 1 × 1 601 DNA Strand 2 × 1 Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone-lysine N-methyltransferase, H3 lysine-79 specific × 1 (Q8TEK3) Ubiquitin × 1 (P0CG48) SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Solutions were prepared on the day of freezing and filtered though a 0.2 um filter prior to use. cryo-EM vitrification conditions:Cryogen ETHANE;Blot once for 3.5 seconds before freezing. Resolution 3.54 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 8
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

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 6nqa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6nqa
Deposition date deposition_date2019-01-19
Structure title titleActive state Dot1L bound to the H2B-Ubiquitinated nucleosome, 1-to-1 complex
Keywords keywordsUbiquitin, Nucleosome, Methyltransferase, STRUCTURAL PROTEIN-TRANSFERASE-DNA complex; STRUCTURAL PROTEIN/TRANSFERASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.43
Radius of gyration Rg (electron density) rg_electron41.57
Forward intensity I(0) i01180990000.00
Molecular weight molecular_weight223020.0 kDa
Excluded volume excluded_volume254150 ų
Envelope volume envelope_volume398930 ų
Hydration-shell volume shell_volume77475 ų
Envelope diameter envelope_diameter136.1
Shell Rg shell_rg49.09
Envelope Rg envelope_rg40.87
Shape Rg shape_rg41.46
Total Rg total_rg42.14
Total atoms total_atoms15322
Residues n_residues1450
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 dmax129.2
Rg (real space) rg_real43.13
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.1810e+09
I(0) uncertainty (real space) i0_real_error2.1480e+07
Rg (reciprocal space) rg_reciprocal43.43
I(0) (reciprocal space) i0_reciprocal1181000000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.4
Skewness Skewness skewness0.018
Kurtosis Kurtosis kurtosis-0.596
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha109600000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.807

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id6nqaA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nqaB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nqaC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nqaD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nqaE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nqaF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nqaG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nqaH00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nqaK01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology260 — 434 Repressor (Amino-terminal Domain)
Homologous superfamily homologous superfamily60
Domain ID domain_id6nqaK02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39

8. Citations (1)

9. Files and Curves (10)