› 4x5z

X-ray diffraction
1.86Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126199 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Menin Chain: A
Molecule details ›
Chain: A
Length: 489 amino acids
Theoretical weight: 54.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00255 (Residues: 1-427, 537-593; Coverage: 74%)
Gene names: MEN1, SCG2
Sequence domains: Menin

Ligands and Environments

5 bound ligands:
Ligand SO4 4 x SO4
Ligand 3XY 1 x 3XY
Ligand PG4 1 x PG4
Ligand DMS 2 x DMS
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 49.013Å b: 80.178Å c: 124.887Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.162 0.208
Expression system: Escherichia coli

Quick links

Citations

91 review citations

Targeting transcription factors in cancer - from undruggable to reality.
Bushweller JH. (2019)
90 more

4 mentions without citation

Pharmacologic inhibition of the Menin-MLL interaction blocks progression of MLL leukemia in vivo.
Borkin et al. (2015)
3 more