PDBe 3u85

X-ray diffraction
3Å resolution

Crystal structure of human menin in complex with MLL1

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Menin Chain: A
Molecule details ›
Chain: A
Length: 550 amino acids
Theoretical weight: 61.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00255 (Residues: 2-615; Coverage: 89%)
  • Best match: O00255-2 (Residues: 2-610)
Gene names: MEN1, SCG2
Sequence domains: Menin
MLL cleavage product N320 Chain: B
Molecule details ›
Chain: B
Length: 21 amino acids
Theoretical weight: 2.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03164 (Residues: 6-25; Coverage: 1%)
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: APS BEAMLINE 21-ID-D
Spacegroup: P41212
Unit cell:
a: 141.205Å b: 141.205Å c: 93.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.22 0.258
Expression systems:
  • Escherichia coli
  • Escherichia coli BL21(DE3)