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The crystal structure of echinococcus granulosus fatty-acid-binding protein 1

Analyse The crystal structure of echinococcus granulosus fatty-acid-binding protein 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1O8V
Type
protein
Length
133 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fatty acid binding protein homolog
UniProt
Q02970
Ligands
ACE, PLM
Pockets
1 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 58% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFatty acid binding protein homologprotein13315% helix, 58% strandQ02970

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A
  • PLM · Palmitic acid · 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
13380.850.9437PLM

Modifications

Observed in the structure: 1 covalent, 1 modified (covalent ligand, oxidation).

Compared structures

  • 1O8V · The crystal structure of Echinococcus granulosus fatty-acid-binding protein 1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q02970 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein homolog 1 (Q02970) · a predicted model of the same protein · chain A against A, TM-score 0.98

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