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Structure of the neurospora set domain protein dim-5, a histone lysine methyltransferase

Analyse Structure of the neurospora set domain protein dim-5, a histone lysine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ML9
Type
protein
Length
260 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone H3 methyltransferase dim-5
EC
2.1.1.43
Ligands
ZN, UNK
Pockets
3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone H3 methyltransferase dim-5 (EC 2.1.1.43)protein26019% helix, 23% strand—

Ligands and binding sites

  • ZN · Zinc ion · metal · 3 copies · chains A
  • UNK · Unknown · ion · 6 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12750.540.7639UNK
21430.440.7621empty
31420.420.7522empty

Compared structures

  • 1ML9 · Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00

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