› 5db3

X-ray diffraction
1.71Å 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: 1-593; Coverage: 79%)
Gene names: MEN1, SCG2
Sequence domains: Menin

Ligands and Environments

5 bound ligands:
Ligand DMS 3 x DMS
Ligand PG4 2 x PG4
Ligand SO4 4 x SO4
Ligand PEG 1 x PEG
Ligand 58Q 1 x 58Q
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 48.899Å b: 80.456Å c: 125.093Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.194
Expression system: Escherichia coli

Quick links

Citations

14 review citations

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

3 mentions without citation

Property Focused Structure-Based Optimization of Small Molecule Inhibitors of the Protein-Protein Interaction between Menin and Mixed Lineage Leukemia (MLL).
Borkin et al. (2016)
2 more