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Crystal structure of the human fatty acid synthase thioesterase domain with an activate site-specific polyunsaturated fatty acyl adduct

Analyse Crystal structure of the human fatty acid synthase thioesterase domain with an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TJM
Type
protein
Length
275 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fatty acid synthase
EC
2.3.1.85, 2.3.1.38, 2.3.1.39, 2.3.1.41, 1.1.1.100, 4.2.1.61, 1.3.1.10, 3.1.2.14
UniProt
P49327
Ligands
7FA
Pockets
1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFatty acid synthase (EC 2.3.1.85, 2.3.1.38, 2.3.1.39, 2.3.1.41, 1.1.1.100, 4.2.1.61, 1.3.1.10, 3.1.2.14)protein27547% helix, 12% strandP49327

Ligands and binding sites

  • 7FA · methyl (R)-(6Z,9Z,12Z)-octadeca-6,9,12-trien-1-ylphosphonofluoridate · ligand · 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
13360.710.83337FA

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 3TJM · Crystal Structure of the Human Fatty Acid Synthase Thioesterase Domain with an Activate… · the same entry in another collection · chain A against A, TM-score 1.00
  • P49327 · AlphaFold monomer V2.0 prediction for fatty acid synthase (P49327) · a predicted model of the same protein · chain A against A, TM-score 0.97

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