6w5i

Cryo-EM structure of MLL1 in complex with RbBP5, WDR5, SET1, and ASH2L bound to the nucleosome (Class01)

Method: ELECTRON MICROSCOPY Dmax: 153.5 Å Quality: GOOD

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

Retinoblastoma-binding protein 5

Homo sapiens

UniProt Q15291

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain A; UniProt 2–538 Not recorded WD repeat-containing protein 5 × 1 (P61964) Histone-lysine N-methyltransferase 2A × 1 (Q03164) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-MER) × 1 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.90 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.

31 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBBP5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–538; UniProt 2–538

WD repeat-containing protein 5

Homo sapiens

UniProt P61964

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain B; UniProt 22–334 Not recorded Retinoblastoma-binding protein 5 × 1 (Q15291) Histone-lysine N-methyltransferase 2A × 1 (Q03164) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-MER) × 1 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.90 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.

198 other PDB entries and 294 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–313; UniProt 22–334

Histone-lysine N-methyltransferase 2A

Homo sapiens

UniProt Q03164

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain C; UniProt 3762–3969 Not recorded Retinoblastoma-binding protein 5 × 1 (Q15291) WD repeat-containing protein 5 × 1 (P61964) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-MER) × 1 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.90 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.

54 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KMT2A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–209; UniProt 3762–3969

Set1/Ash2 histone methyltransferase complex subunit ASH2

Homo sapiens

UniProt Q9UBL3

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain D; UniProt 2–534 Not recorded Retinoblastoma-binding protein 5 × 1 (Q15291) WD repeat-containing protein 5 × 1 (P61964) Histone-lysine N-methyltransferase 2A × 1 (Q03164) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-MER) × 1 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.90 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.

31 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASH2L_HUMAN
Isoform Q9UBL3-3
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–534; UniProt 2–534

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain G; UniProt 1–136 Chain K; UniProt 1–136 Not recorded Retinoblastoma-binding protein 5 × 1 (Q15291) WD repeat-containing protein 5 × 1 (P61964) Histone-lysine N-methyltransferase 2A × 1 (Q03164) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-MER) × 1 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.90 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 5
Chains and sequence ranges Author chain G; PDBConstruct 1–136; UniProt 1–136 Author chain K; 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 Protein–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain H; UniProt 1–103 Chain L; UniProt 1–103 Not recorded Retinoblastoma-binding protein 5 × 1 (Q15291) WD repeat-containing protein 5 × 1 (P61964) Histone-lysine N-methyltransferase 2A × 1 (Q03164) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.2 × 2 (P84233) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (147-MER) × 1 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.90 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 6
Chains and sequence ranges Author chain H; PDBConstruct 1–103; UniProt 1–103 Author chain L; PDBConstruct 1–103; UniProt 1–103

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain I; UniProt 2–130 Chain M; UniProt 2–130 Not recorded Retinoblastoma-binding protein 5 × 1 (Q15291) WD repeat-containing protein 5 × 1 (P61964) Histone-lysine N-methyltransferase 2A × 1 (Q03164) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (147-MER) × 1 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.90 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 7
Chains and sequence ranges Author chain I; PDBConstruct 4–132; UniProt 2–130 Author chain M; PDBConstruct 4–132; 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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain J; UniProt 5–126 Chain N; UniProt 5–126 Not recorded Retinoblastoma-binding protein 5 × 1 (Q15291) WD repeat-containing protein 5 × 1 (P61964) Histone-lysine N-methyltransferase 2A × 1 (Q03164) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) DNA (147-MER) × 1 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.90 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 8
Chains and sequence ranges Author chain J; PDBConstruct 1–122; UniProt 5–126 Author chain N; PDBConstruct 1–122; UniProt 5–126

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 6w5i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6w5i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6w5i
Deposition date deposition_date2020-03-13
Structure title titleCryo-EM structure of MLL1 in complex with RbBP5, WDR5, SET1, and ASH2L bound to the nucleosome (Class01)
Keywords keywordsMLL1-NCP, H3K4 methylation, TRANSFERASE, TRANSFERASE-STRUCTURAL PROTEIN-DNA complex; TRANSFERASE/STRUCTURAL PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.01
Radius of gyration Rg (electron density) rg_electron47.25
Forward intensity I(0) i01721520000.00
Molecular weight molecular_weight284860.0 kDa
Excluded volume excluded_volume331420 ų
Envelope volume envelope_volume501300 ų
Hydration-shell volume shell_volume86955 ų
Envelope diameter envelope_diameter152.5
Shell Rg shell_rg53.72
Envelope Rg envelope_rg45.58
Shape Rg shape_rg47.24
Total Rg total_rg47.49
Total atoms total_atoms19669
Residues n_residues2033
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 dmax153.5
Rg (real space) rg_real47.69
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real1.7220e+09
I(0) uncertainty (real space) i0_real_error3.0510e+07
Rg (reciprocal space) rg_reciprocal48.01
I(0) (reciprocal space) i0_reciprocal1722000000.0000
Solution quality estimate total_estimate0.8178
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.1
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.501
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha126400000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)