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Crystal structure of SAM-dependent methyltransferase, possible histamine N-methyltransferase (TM1293) from thermotoga maritima at 2.20 a resolution

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

PDB
1VLM
Type
protein
Length
414 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SAM-dependent methyltransferase
UniProt
Q9X119
Ligands
NA
Pockets
2 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASAM-dependent methyltransferaseprotein20737% helix, 24% strandQ9X119
BSAM-dependent methyltransferaseprotein20739% helix, 23% strandQ9X119

Ligands and binding sites

  • 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13380.770.8855empty
23310.760.8743empty

Interfaces

1 interface between chains.

  • A–B · 38 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 1VLM · Crystal structure of SAM-dependent methyltransferase, possible histamine… · the same entry in another collection · chain A against A, TM-score 1.00

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