7w67

The crystal structure of MLL1 (N3861I/Q3867L/C3882SS)-RBBP5-ASH2L in complex with H3K4me0 peptide

Method: X-RAY DIFFRACTION Dmax: 81.6 Å Quality: GOOD

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

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 380–496 Chain A; UniProt 539–598 Not recorded Histone-lysine N-methyltransferase 2A × 1 (Q03164) Retinoblastoma-binding protein 5 × 1 (Q15291) Histone H3.3C × 1 (Q6NXT2) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M Sodium chloride, 0.1 M HEPES, pH 7.5, 25% w/v polyethylene glycol 3350 Resolution 2.19 Å R-free 0.222

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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–118; UniProt 380–496 Author chain A; PDBConstruct 125–184; UniProt 539–598

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 3813–3969 Mutation:N3861I,Q3867L,C3882SS Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Retinoblastoma-binding protein 5 × 1 (Q15291) Histone H3.3C × 1 (Q6NXT2) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M Sodium chloride, 0.1 M HEPES, pH 7.5, 25% w/v polyethylene glycol 3350 Resolution 2.19 Å R-free 0.222

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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–158; UniProt 3813–3969

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 330–356 Not recorded Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone-lysine N-methyltransferase 2A × 1 (Q03164) Histone H3.3C × 1 (Q6NXT2) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M Sodium chloride, 0.1 M HEPES, pH 7.5, 25% w/v polyethylene glycol 3350 Resolution 2.19 Å R-free 0.222

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 3
Chains and sequence ranges Author chain F; PDBConstruct 1–27; UniProt 330–356

Histone H3.3C

OrganismNot specified

UniProt Q6NXT2

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 2–10 Not recorded Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone-lysine N-methyltransferase 2A × 1 (Q03164) Retinoblastoma-binding protein 5 × 1 (Q15291) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M Sodium chloride, 0.1 M HEPES, pH 7.5, 25% w/v polyethylene glycol 3350 Resolution 2.19 Å R-free 0.222

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.

22 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3C_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 1–9; UniProt 2–10

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 7w67

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7w67
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7w67
Deposition date deposition_date2021-12-01
Structure title titleThe crystal structure of MLL1 (N3861I/Q3867L/C3882SS)-RBBP5-ASH2L in complex with H3K4me0 peptide
Keywords keywordsMLL family methyltransferases, product specificity, F/Y switch, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.30
Radius of gyration Rg (electron density) rg_electron24.47
Forward intensity I(0) i028949500.00
Molecular weight molecular_weight41391.0 kDa
Excluded volume excluded_volume51748 ų
Envelope volume envelope_volume63671 ų
Hydration-shell volume shell_volume22320 ų
Envelope diameter envelope_diameter84.0
Shell Rg shell_rg31.08
Envelope Rg envelope_rg24.17
Shape Rg shape_rg24.42
Total Rg total_rg25.43
Total atoms total_atoms2909
Residues n_residues360
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 dmax81.6
Rg (real space) rg_real25.36
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real2.8950e+07
I(0) uncertainty (real space) i0_real_error3.7740e+05
Rg (reciprocal space) rg_reciprocal25.35
I(0) (reciprocal space) i0_reciprocal28950000.0000
Solution quality estimate total_estimate0.8803
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.617
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7413000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.883; Smooth: 0.958

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)