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Crystal structure of human menin

Analyse Crystal structure of human menin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3U84
Type
protein
Length
978 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Menin
UniProt
O00255
Pockets
11 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMeninprotein50655% helix, 7% strandO00255
BMeninprotein47255% helix, 7% strandO00255

Pockets

11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17090.720.7869empty
26740.670.7653empty
3820.390.7821empty
4790.360.7618empty
5870.330.7415empty

Interfaces

1 interface between chains.

  • A–B · 194 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3U84 · Crystal Structure of Human Menin · the same entry in another collection · chain A against A, TM-score 1.00
  • O00255 · AlphaFold monomer V2.0 prediction for menin (O00255) · a predicted model of the same protein · chain B against A, TM-score 0.98

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