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Crystal structure of tRNA (UM34/CM34) methyltransferase trml from escherichia COLI with sah

Analyse Crystal structure of tRNA (UM34/CM34) methyltransferase trml from escherichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4JAL
Type
protein
Length
311 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRNA (CYTIDINE(34)-2'-O)-methyltransferase
EC
2.1.1.207
UniProt
P0AGJ7
Ligands
SAH
Pockets
1 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATRNA (CYTIDINE(34)-2'-O)-methyltransferase (EC 2.1.1.207)protein15636% helix, 18% strandP0AGJ7
BTRNA (CYTIDINE(34)-2'-O)-methyltransferase (EC 2.1.1.207)protein15536% helix, 18% strandP0AGJ7

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 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
16350.750.8183SAH, EPE, EDO

Interfaces

1 interface between chains.

  • A–B · 1389 Ų buried · 32 hydrogen bonds · protein-protein

Compared structures

  • 4JAL · Crystal structure of tRNA (Um34/Cm34) methyltransferase TrmL from Escherichia coli with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0AGJ7 · AlphaFold monomer V2.0 prediction for tRNA (CYTIDINE(34)-2'-O)-methyltransferase (P0AGJ7) · a predicted model of the same protein · chain A against A, TM-score 0.98

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