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Crystal structure of SAM-dependent methyltransferase from thiobacillus denitrificans in complex with S-adenosyl-L-homocysteine

Analyse Crystal structure of SAM-dependent methyltransferase from thiobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5EPE
Type
protein
Length
248 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SAM-dependent methyltransferase
EC
2.1.1.-
UniProt
Q3SJX0
Ligands
SAH, NA
Pockets
2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASAM-dependent methyltransferase (EC 2.1.1.-)protein24847% helix, 23% strandQ3SJX0

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · chains A
  • NA · Sodium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15900.730.8058SAH
2500.280.7512empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 5EPE · Crystal structure of SAM-dependent methyltransferase from Thiobacillus denitrificans in… · the same entry in another collection · chain A against A, TM-score 1.00

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