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The ligand-free structure of gfsa ksq-at didomain

Analyse The ligand-free structure of gfsa ksq-at didomain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VEE
Type
protein
Length
828 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polyketide synthase
Pockets
9 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolyketide synthaseprotein82843% helix, 19% strand—

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.710.9817empty
24360.690.8054empty
33370.680.8240empty
41960.630.8333empty
5960.410.7719empty

Compared structures

  • 7VEE · The ligand-free structure of GfsA KSQ-AT didomain · the same entry in another collection · chain A against A, TM-score 1.00

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