› 7w6i

X-ray diffraction
2.56Å resolution

The crystal structure of MLL1 (N3861I/Q3867L/C3882SS)-RBBP5-ASH2L in complex with H3K4me1 peptide

Released:
DOI: 10.2210/pdb7w6i/pdb
Model geometry
Fit model/data
PDB entry 7w6i coloured by chain, front view.
PDB entry 7w6i coloured by chain, side view.
PDB entry 7w6i coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for product specificities of MLL family methyltransferases.
Li Y, Zhao L, Zhang Y, Wu P, Xu Y, Mencius J, Zheng Y, Wang X, Xu W, Huang N, Ye X, Lei M, Shi P, Tian C, Peng C, Li G, Liu Z, Quan S, Chen Y
Mol Cell (2022)
PMID: 36108631

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-169857 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Set1/Ash2 histone methyltransferase complex subunit ASH2 Chain: A
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 20.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBL3 (Residues: 380-496, 516-598; Coverage: 28%)
Gene names: ASH2L, ASH2L1
Sequence domains: SPRY domain
MLL cleavage product C180 Chain: C
Molecule details ›
Chain: C
Length: 159 amino acids
Theoretical weight: 18.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03164 (Residues: 3813-3881, 3882-3969; Coverage: 4%)
Gene names: ALL1, CXXC7, HRX, HTRX, KMT2A, MLL, MLL1, TRX1
Sequence domains: SET domain
Retinoblastoma-binding protein 5 Chain: F
Histone H3.3C Chain: B

Ligands and Environments

2 bound ligands:
Ligand SAH 1 x SAH
Ligand ZN 1 x ZN
1 modified residue:
Ligand MLZ 1 x MLZ

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: C2
Unit cell:
a: 75.777Å b: 44.422Å c: 120.097Å
α: 90° β: 107.51° γ: 90°
R-values:
R R work R free
0.202 0.198 0.244
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 citations in other articles

KMT2A maintains stemness of gastric cancer cells through regulating Wnt/β-catenin signaling-activated transcriptional factor KLF11.
Deng et al. (2023)