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Crystal structure of lysk from thermus thermophilus in complex with lysine

Analyse Crystal structure of lysk from thermus thermophilus in complex with lysine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XOY
Type
protein
Length
690 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
[lysw]-lysine hydrolase
EC
3.5.1.-
UniProt
Q8VUS5
Ligands
LYS, SO4
Pockets
3 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A[lysw]-lysine hydrolase (EC 3.5.1.-)protein34136% helix, 28% strandQ8VUS5
B[lysw]-lysine hydrolase (EC 3.5.1.-)protein34934% helix, 29% strandQ8VUS5

Ligands and binding sites

  • LYS · Lysine · ligand · chains A, B
  • SO4 · Sulfate ion · ion · 3 copies · chains A, B

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
13750.720.8362LYS
25810.650.7657empty
3840.440.8020empty

Interfaces

1 interface between chains.

  • A–B · 1292 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 5XOY · Crystal structure of LysK from Thermus thermophilus in complex with Lysine · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8VUS5 · AlphaFold monomer V2.0 prediction for [lysw]-lysine hydrolase (Q8VUS5) · a predicted model of the same protein · chain B against A, TM-score 0.99

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