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Crystal structure of adomet bound rRNA methyltransferase from sinorhizobium meliloti

Analyse Crystal structure of adomet bound rRNA methyltransferase from sinorhizobium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5L0Z
Type
protein
Length
523 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Probable RNA methyltransferase, trmh family
EC
2.1.1.-
UniProt
Q92SJ4
Ligands
SAM, CO, SO4
Pockets
4 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProbable RNA methyltransferase, trmh family (EC 2.1.1.-)protein26238% helix, 22% strandQ92SJ4
BProbable RNA methyltransferase, trmh family (EC 2.1.1.-)protein26138% helix, 21% strandQ92SJ4

Ligands and binding sites

  • SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
  • CO · Cobalt (II) ion · metal · 4 copies · chains A, B
  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15910.740.8166SO4, SAM
21470.440.7626empty
3760.410.7918empty
4580.320.7613empty

Interfaces

1 interface between chains.

  • A–B · 1381 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 5L0Z · Crystal Structure of AdoMet bound rRNA methyltransferase from Sinorhizobium meliloti · the same entry in another collection · chain A against A, TM-score 1.00

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