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Crystal structure of histone methyltransferase SET7/9 in complex with daam-3

Analyse Crystal structure of histone methyltransferase SET7/9 in complex with daam-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VV0
Type
protein
Length
235 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone-lysine N-methyltransferase SETD7
EC
2.1.1.43
UniProt
Q8WTS6
Ligands
KH3
Pockets
1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone-lysine N-methyltransferase SETD7 (EC 2.1.1.43)protein23511% helix, 40% strandQ8WTS6

Ligands and binding sites

  • KH3 · 5'-{[(3S)-3-amino-3-carboxypropyl][2-(hexylamino)ethyl]amino}-5'-deoxyadenosine · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12290.520.7632KH3

Compared structures

  • 3VV0 · Crystal structure of histone methyltransferase SET7/9 in complex with DAAM-3 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8WTS6 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD7 (Q8WTS6) · a predicted model of the same protein · chain A against A, TM-score 0.99

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