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Crystal structure of human METTL1 bound to sinefungin

Analyse Crystal structure of human METTL1 bound to sinefungin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7PL1
Type
protein
Length
210 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRNA (guanine-N(7)-)-methyltransferase
EC
2.1.1.33, 2.1.1.-
UniProt
Q9UBP6
Ligands
SFG, SO4
Pockets
2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.33, 2.1.1.-)protein21035% helix, 22% strandQ9UBP6

Ligands and binding sites

  • SFG · Sinefungin · ligand · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
  • GOL · Glycerol · 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
11870.490.7630SFG
2730.380.7718GOL

Compared structures

  • 7PL1 · Crystal structure of human METTL1 bound to Sinefungin · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UBP6 · AlphaFold monomer V2.0 prediction for tRNA (guanine-N(7)-)-methyltransferase (Q9UBP6) · a predicted model of the same protein · chain A against A, TM-score 0.94

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