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Crystal structure of leut bound to L-selenomethionine in space group C2 from lipid bicelles

Analyse Crystal structure of leut bound to L-selenomethionine in space group C2 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3USL
Type
protein
Length
502 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transporter
UniProt
O67854
Ligands
MSE, PC, NA, IOD
Pockets
3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransporterprotein50279% helix, 1% strandO67854

Ligands and binding sites

  • MSE · Selenomethionine · ligand · chains A
  • PC · Phosphocholine · ligand · chains A
  • NA · Sodium ion · metal · 2 copies · chains A
  • IOD · Iodide ion · ion · chains A
  • ACT · Acetate ion · additive · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15610.690.7859empty
2770.520.8516IOD
31190.390.7311empty

Compared structures

  • 3USL · Crystal Structure of LeuT bound to L-selenomethionine in space group C2 from lipid… · the same entry in another collection · chain A against A, TM-score 1.00

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