9yle

State 3 MLL4FC bound to a nucleosome premodified with H2BK120ub and H4K16ac

Method: ELECTRON MICROSCOPY Dmax: 195.4 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 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain O; UniProt 1–76 Not recorded [histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D × 1 (A0A6P6IDI8,O14686) Retinoblastoma-binding protein 5 × 1 (Q15291) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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 O; PDBConstruct 1–76; UniProt 1–76

[histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D

Homo sapiens

UniProt A0A6P6IDI8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain K; UniProt 1102–1316 Not recorded Ubiquitin × 1 (P0CG47) Retinoblastoma-binding protein 5 × 1 (Q15291) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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 A0A6P6IDI8_PUMCO
Isoform
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 11–225; UniProt 1102–1316

[histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D

Homo sapiens

UniProt O14686

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain K; UniProt 4507–5537 Not recorded Ubiquitin × 1 (P0CG47) Retinoblastoma-binding protein 5 × 1 (Q15291) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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.

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KMT2D_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 226–1256; UniProt 4507–5537

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 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain N; UniProt 1–538 Not recorded Ubiquitin × 1 (P0CG47) [histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D × 1 (A0A6P6IDI8,O14686) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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 3
Chains and sequence ranges Author chain N; PDBConstruct 1–538; UniProt 1–538

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 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain T; UniProt 1–628 Not recorded Ubiquitin × 1 (P0CG47) [histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D × 1 (A0A6P6IDI8,O14686) Retinoblastoma-binding protein 5 × 1 (Q15291) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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
PDB entities 4
Chains and sequence ranges Author chain T; PDBConstruct 1–628; UniProt 1–628

Histone H3.1

Homo sapiens

UniProt P68431

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Ubiquitin × 1 (P0CG47) [histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D × 1 (A0A6P6IDI8,O14686) Retinoblastoma-binding protein 5 × 1 (Q15291) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

Histone H4

Homo sapiens

UniProt P62805

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded Ubiquitin × 1 (P0CG47) [histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D × 1 (A0A6P6IDI8,O14686) Retinoblastoma-binding protein 5 × 1 (Q15291) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 6
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-B/E

Homo sapiens

UniProt P04908

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Ubiquitin × 1 (P0CG47) [histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D × 1 (A0A6P6IDI8,O14686) Retinoblastoma-binding protein 5 × 1 (Q15291) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B type 2-E

Homo sapiens

UniProt Q16778

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain D; UniProt 2–126 Chain H; UniProt 2–126 Not recorded Ubiquitin × 1 (P0CG47) [histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D × 1 (A0A6P6IDI8,O14686) Retinoblastoma-binding protein 5 × 1 (Q15291) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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.

39 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B2E_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

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 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain R; UniProt 1–334 Not recorded Ubiquitin × 1 (P0CG47) [histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D × 1 (A0A6P6IDI8,O14686) Retinoblastoma-binding protein 5 × 1 (Q15291) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 DNA (145-MER) × 1 Protein dpy-30 homolog × 2 (Q9C005) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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 10
Chains and sequence ranges Author chain R; PDBConstruct 1–334; UniProt 1–334

Protein dpy-30 homolog

Homo sapiens

UniProt Q9C005

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain P; UniProt 1–99 Chain Q; UniProt 1–99 Not recorded Ubiquitin × 1 (P0CG47) [histone H3]-lysine(4) N-methyltransferase,Histone-lysine N-methyltransferase 2D × 1 (A0A6P6IDI8,O14686) Retinoblastoma-binding protein 5 × 1 (Q15291) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 2-E × 2 (Q16778) DNA (145-MER) × 1 WD repeat-containing protein 5 × 1 (P61964) DNA (145-MER) × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.63 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.

11 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPY30_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain P; PDBConstruct 1–99; UniProt 1–99 Author chain Q; PDBConstruct 1–99; UniProt 1–99

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 9yle

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yle
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yle
Deposition date deposition_date2025-10-08
Structure title titleState 3 MLL4FC bound to a nucleosome premodified with H2BK120ub and H4K16ac
Keywords keywordsMLL4 complex, histone modification, nucleosome recognition, transcription coactivation, TRANSCRIPTION, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.66
Radius of gyration Rg (electron density) rg_electron57.85
Forward intensity I(0) i02839350000.00
Molecular weight molecular_weight385160.0 kDa
Excluded volume excluded_volume456500 ų
Envelope volume envelope_volume775790 ų
Hydration-shell volume shell_volume112720 ų
Envelope diameter envelope_diameter210.2
Shell Rg shell_rg61.49
Envelope Rg envelope_rg56.33
Shape Rg shape_rg57.85
Total Rg total_rg57.95
Total atoms total_atoms26696
Residues n_residues2908
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 dmax195.4
Rg (real space) rg_real57.60
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real2.8390e+09
I(0) uncertainty (real space) i0_real_error5.8340e+07
Rg (reciprocal space) rg_reciprocal57.70
I(0) (reciprocal space) i0_reciprocal2840000000.0000
Solution quality estimate total_estimate0.8613
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary72.4
Skewness Skewness skewness0.337
Kurtosis Kurtosis kurtosis-0.097
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha192600000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.801; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.791

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)