› 5dde

X-ray diffraction
1.78Å resolution

Menin in complex with MI-859

Released:
DOI: 10.2210/pdb5dde/pdb
PDB entry 5dde coloured by chain, front view.
PDB entry 5dde coloured by chain, side view.
PDB entry 5dde coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Rational Design of Orthogonal Multipolar Interactions with Fluorine in Protein-Ligand Complexes.
Pollock J, Borkin D, Lund G, Purohit T, Dyguda-Kazimierowicz E, Grembecka J, Cierpicki T
J Med Chem 58 7465-74 (2015)
PMID: 26288158

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 5A0 2 x 5A0
Ligand SO4 4 x SO4
Ligand DMS 4 x DMS
Ligand PG4 1 x PG4
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: 48.705Å b: 79.713Å c: 124.644Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 0.199
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Dissecting the Structure-Activity Relationship of Galectin-Ligand Interactions.
Chan et al. (2018)
2 more

1 mention without citation

Using Structural Analysis In Silico to Assess the Impact of Missense Variants in MEN1.
Caswell et al. (2019)