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Crystal structure of a N-myc downstream regulated 2 protein (NDRG2, syld, NDR2, AI182517, AU040374) from mus musculus at 1.70 a resolution

Analyse Crystal structure of a N-myc downstream regulated 2 protein (NDRG2, syld, NDR2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QMQ
Type
protein
Length
278 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein NDRG2
UniProt
Q9QYG0
Ligands
BEZ, MG
Pockets
2 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein NDRG2protein27844% helix, 20% strandQ9QYG0

Ligands and binding sites

  • BEZ · Benzoic acid · ligand · chains A
  • MG · Magnesium ion · metal · 2 copies · chains A
  • 2PE · Nonaethylene glycol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11630.440.7523empty
2720.320.7414empty

Compared structures

  • 2QMQ · Crystal structure of a n-myc downstream regulated 2 protein (ndrg2, syld, ndr2, ai182517… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9QYG0 · AlphaFold monomer V2.0 prediction for protein NDRG2 (Q9QYG0) · a predicted model of the same protein · chain A against A, TM-score 0.98

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