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Crystal structure of rsmd methyltransferase of M. tuberculosis in complex with sinefungin reveals key interactions

Analyse Crystal structure of rsmd methyltransferase of M. tuberculosis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6M1C
Type
protein
Length
184 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Possible methyltransferase (methylase)
UniProt
I6XFS7
Ligands
SFG
Pockets
1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APossible methyltransferase (methylase)protein18430% helix, 23% strandI6XFS7

Ligands and binding sites

  • SFG · Sinefungin · ligand · chains A
  • ACT · Acetate ion · 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
12510.610.8038SFG, ACT

Compared structures

  • 6M1C · Crystal structure of RsmD methyltransferase of M. tuberculosis in complex with sinefungin… · the same entry in another collection · chain A against A, TM-score 1.00

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