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Crystal structure of C21orf127-TRMT112 in complex with SAH

Analyse Crystal structure of C21orf127-TRMT112 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
6H1D
Type
protein
Length
322 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.94
Source
Homo sapiens
Molecule
HemK methyltransferase family member 2; Multifunctional methyltransferase subunit…
EC
2.1.1.-
UniProt
Q9Y5N5, Q9UI30
Ligands
SAH
Pockets
3 · best druggability 0.78

Structure

x-ray diffraction · resolution 1.94 · 2 distinct chains · 37% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHemK methyltransferase family member 2 (EC 2.1.1.-)protein20738% helix, 26% strandQ9Y5N5
BMultifunctional methyltransferase subunit TRM112-like proteinprotein11535% helix, 23% strandQ9UI30

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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11940.780.9342SAH
2970.590.8622empty
31950.510.7725empty

Interfaces

1 interface between chains.

  • A–B · 1210 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 6H1D · Crystal structure of C21ORF127-TRMT112 in complex with sah · 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 0.97

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