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The structure of the human METTL6 enzyme in complex with sah

Analyse The structure of the human METTL6 enzyme in complex with sah in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EZG
Type
protein
Length
275 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRNA N(3)-methylcytidine methyltransferase METTL6
EC
2.1.1.-
UniProt
Q8TCB7
Ligands
SAH
Pockets
2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATRNA N(3)-methylcytidine methyltransferase METTL6 (EC 2.1.1.-)protein27536% helix, 25% strandQ8TCB7

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16910.760.8181SAH
2730.480.8315empty

Compared structures

  • 7EZG · The structure of the human METTL6 enzyme in complex with SAH · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8TCB7 · AlphaFold monomer V2.0 prediction for tRNA N(3)-methylcytidine methyltransferase METTL6… · a predicted model of the same protein · chain A against A, TM-score 0.89

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