9yle

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

Method: ELECTRON MICROSCOPY
▼

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

Ubiquitin

Homo sapiens

UniProt P0CG47

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 [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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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) water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 15 DNA 2 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 water × 11 Consistent with all polymers

Other States of the Same Protein in the Database

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.

▼

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. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

9yle__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9yle__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9yle__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)57.66 Å
Rg (electron density)57.85 Å
Total Rg57.95 Å
Atom count26696
Residues2908
Excluded volume456500 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9yle__assembly_1__model_1 17-meric (17) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (13)

▶

7. Citations (1)