› 3u84

X-ray diffraction
2.5Å resolution

Crystal Structure of Human Menin

Released:
DOI: 10.2210/pdb3u84/pdb
PDB entry 3u84 coloured by chain, front view.
PDB entry 3u84 coloured by chain, side view.
PDB entry 3u84 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The same pocket in menin binds both MLL and JUND but has opposite effects on transcription.
Huang J, Gurung B, Wan B, Matkar S, Veniaminova NA, Wan K, Merchant JL, Hua X, Lei M
Nature 482 542-6 (2012)
PMID: 22327296

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-126199 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Menin Chains: A, B
Molecule details ›
Chains: A, B
Length: 550 amino acids
Theoretical weight: 61.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O00255 (Residues: 2-610; Coverage: 90%)
Gene names: MEN1, SCG2
Sequence domains: Menin

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: P41
Unit cell:
a: 139.891Å b: 139.891Å c: 54.146Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.236
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

53 review citations

Epigenetic modifications of histones in cancer.
Zhao et al. (2019)
52 more

16 mentions without citation

Challenges and opportunities in targeting the menin-MLL interaction.
Cierpicki et al. (2014)
15 more