PDBe 3p4f

X-ray diffraction
2.35Å resolution

Structural and biochemical insights into MLL1 core complex assembly and regulation.

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
WD repeat-containing protein 5 Chain: A
Molecule details ›
Chain: A
Length: 317 amino acids
Theoretical weight: 34.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61964 (Residues: 22-334; Coverage: 94%)
Gene names: BIG3, WDR5
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Retinoblastoma-binding protein 5 Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.28 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15291 (Residues: 371-381; Coverage: 2%)
Gene names: RBBP5, RBQ3
MLL cleavage product C180 Chain: C
Molecule details ›
Chain: C
Length: 10 amino acids
Theoretical weight: 1.06 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q03164 (Residues: 3761-3770; Coverage: 0%)
Gene names: ALL1, CXXC7, HRX, HTRX, KMT2A, MLL, MLL1, TRX1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 53.85Å b: 81.35Å c: 81.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.249
Expression systems:
  • Escherichia coli
  • Not provided