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Crystal structure of a putative class I S-adenosylmethionine-dependent methyltransferase (LMO1582) from listeria monocytogenes at 2.20 a resolution

Analyse Crystal structure of a putative class I S-adenosylmethionine-dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F8L
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein LMO1582
Ligands: SAM, CL, SO4
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein LMO1582	protein	323	47% helix, 19% strand	—

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A
CL · Chloride ion · ion · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 5 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	173	0.59	0.82	37	SAM
2	90	0.39	0.77	17	empty
3	52	0.38	0.79	13	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

2F8L · Crystal structure of a putative class i s-adenosylmethionine-dependent methyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 2F8L · PDBe 2F8L

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