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Geranyl pyrophosphate C6-methyltransferase beza

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

PDB
7FBH
Type
protein
Length
823 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beza
Ligands
LYS
Pockets
7 · best druggability 0.77

Structure

x-ray diffraction · 3 distinct chains · 49% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABezaprotein27649% helix, 20% strand—
BBezaprotein27249% helix, 19% strand—
CBezaprotein27549% helix, 19% strand—

Ligands and binding sites

  • LYS · Lysine · ligand · 2 copies · chains B, C
  • GOL · Glycerol · additive · 5 copies · chains A, B, C
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 3 copies · chains A, B, C
  • EDO · 1,2-ethanediol · additive · 3 copies · chains 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, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16280.770.8360EPE, GOL
25700.760.8360EPE
35290.750.8357EPE
45280.690.7968GOL
53510.640.7939GOL

Interfaces

3 interfaces between chains.

  • A–C · 531 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 339 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 133 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 7FBH · geranyl pyrophosphate C6-methyltransferase BezA · the same entry in another collection · chain A against A, TM-score 1.00

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