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Crystal structure of the long-chain fatty acid transporter fadl mutant delta N3

Analyse Crystal structure of the long-chain fatty acid transporter fadl mutant delta N3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2R89
Type
protein
Length
726 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Long-chain fatty acid transport protein
UniProt
P10384
Pockets
4 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 57% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLong-chain fatty acid transport proteinprotein3639% helix, 57% strandP10384

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111880.860.86105empty
28440.820.8477empty
33830.620.7837empty
43360.590.7735empty

Interfaces

1 interface between chains.

  • A–B · 638 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 2R89 · Crystal structure of the long-chain fatty acid transporter FadL mutant delta N3 · the same entry in another collection · chain A against A, TM-score 1.00
  • P10384 · AlphaFold monomer V2.0 prediction for long-chain fatty acid transport protein (P10384) · a predicted model of the same protein · chain B against A, TM-score 0.99

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