GL1X · GenesisL1 explorer

Research workbench

Structural basis of acyl transfer in a trans-at polyketide synthase

Analyse Structural basis of acyl transfer in a trans-at polyketide synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DZ7
Type
protein
Length
281 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polyketide biosynthesis protein pkse
EC
2.3.1.39
UniProt
O34787
Ligands
CL
Pockets
1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolyketide biosynthesis protein pkse (EC 2.3.1.39)protein28147% helix, 15% strandO34787

Ligands and binding sites

  • CL · Chloride ion · ion · chains A
  • GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12520.610.8034GOL

Compared structures

  • 5DZ7 · Structural basis of acyl transfer in a trans-at polyketide synthase · the same entry in another collection · chain A against A, TM-score 1.00
  • O34787 · AlphaFold monomer V2.0 prediction for polyketide biosynthesis protein pkse (O34787) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.