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Crystal structure of HEMK2-TRMT112 complex

Analyse Crystal structure of HEMK2-TRMT112 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PED
Type
protein
Length
319 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methyltransferase N6AMT1; Multifunctional methyltransferase subunit TRM112-like protein
EC
2.1.1.-, 2.1.1.72
UniProt
Q9Y5N5, Q9UI30
Ligands
SAH, UNX
Pockets
3 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMethyltransferase N6AMT1 (EC 2.1.1.-, 2.1.1.72)protein19338% helix, 28% strandQ9Y5N5
BMultifunctional methyltransferase subunit TRM112-like proteinprotein12632% helix, 22% strandQ9UI30

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · chains A
  • UNX · Unknown atom or ion · ion · 12 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12150.770.9143SAH, UNX
2890.550.8521UNX
3550.340.7816empty

Interfaces

1 interface between chains.

  • A–B · 1141 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6PED · Crystal structure of HEMK2-TRMT112 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9Y5N5 · AlphaFold monomer V2.0 prediction for methyltransferase N6AMT1 (Q9Y5N5) · a predicted model of the same protein · chain A against A, TM-score 0.99
  • Q9UI30 · AlphaFold monomer V2.0 prediction for multifunctional methyltransferase subunit… · a predicted model of the same protein · chain B against A, TM-score 0.94

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