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Geranyl pyrophosphate C6-methyltransferase beza binding with S- adenosylhomocysteine

Analyse Geranyl pyrophosphate C6-methyltransferase beza binding with S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7FBO
Type
protein
Length
845 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beza
Ligands
SAH
Pockets
7 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CBezaprotein28250% helix, 20% strand—
BBezaprotein28149% helix, 19% strand—

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · 3 copies · chains A, B, C
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 3 copies · chains A, B, C

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

Pockets

7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13580.820.9163EPE, SAH
24080.810.8965SAH, EPE
34090.810.8963SAH, EPE
43610.600.7744empty
53090.590.7840empty

Interfaces

3 interfaces between chains.

  • A–C · 594 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 312 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 232 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 7FBO · geranyl pyrophosphate C6-methyltransferase BezA binding with S-adenosylhomocysteine · the same entry in another collection · chain A against A, TM-score 1.00

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