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Lccomt in complex with SAM

Analyse Lccomt in complex with SAM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7V6J
Type
protein
Length
687 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lccomt
Ligands
SAM, NA
Pockets
9 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALccomtprotein34651% helix, 16% strand—
BLccomtprotein34149% helix, 17% strand—

Ligands and binding sites

  • SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
  • NA · Sodium ion · metal · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19210.780.8064SAM
28700.780.8163SAM
31850.570.8019empty
41590.450.7633empty
51310.410.7526empty

Interfaces

1 interface between chains.

  • A–B · 4441 Ų buried · 48 hydrogen bonds · protein-protein

Compared structures

  • 7V6J · LcCOMT in complex with SAM · the same entry in another collection · chain A against A, TM-score 1.00

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