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Three-dimensional structures of the periplasmic lysine-, arginine-, ornithine-binding protein with and without a ligand

Analyse Three-dimensional structures of the periplasmic lysine-, arginine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1LST
Type
protein
Length
238 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lysine, arginine, ornithine-binding protein
UniProt
P02911
Ligands
LYS
Pockets
1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALysine, arginine, ornithine-binding proteinprotein23839% helix, 22% strandP02911

Ligands and binding sites

  • LYS · Lysine · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1860.420.7817empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1LST · Three-dimensional structures of the periplasmic lysine-, arginine-, ornithine-binding… · the same entry in another collection · chain A against A, TM-score 1.00
  • P02911 · AlphaFold monomer V2.0 prediction for LYSINE/ARGININE/ORNITHINE- binding periplasmic… · a predicted model of the same protein · chain A against A, TM-score 1.00

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