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Crystal structure of SAM-dependent methyltransferase (ZP_00538691.1) from exiguobacterium sp. 255-15 at 1.90 a resolution

Analyse Crystal structure of SAM-dependent methyltransferase (ZP_00538691.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3D2L
Type
protein
Length
956 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SAM-dependent methyltransferase
UniProt
Q41FK2
Ligands
MG
Pockets
10 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, DSAM-dependent methyltransferaseprotein23830% helix, 36% strandQ41FK2
CSAM-dependent methyltransferaseprotein24231% helix, 33% strandQ41FK2

Ligands and binding sites

  • MG · Magnesium ion · metal · 6 copies · chains A, B, D, C

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

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15950.750.8159empty
26340.750.8157empty
36060.740.8060empty
46370.730.8057empty
51840.500.7723MG

Interfaces

3 interfaces between chains.

  • A–D · 391 Ų buried · 5 hydrogen bonds · protein-protein
  • C–D · 286 Ų buried · 3 hydrogen bonds · protein-protein
  • B–D · 20 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 21 modified (engineered).

Compared structures

  • 3D2L · Crystal structure of SAM-dependent methyltransferase (ZP_00538691.1) from EXIGUOBACTERIUM… · the same entry in another collection · chain A against A, TM-score 1.00

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