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Structure of the conserved yeast listerin (Ltn1) N-terminal domain, MONOCLINIC FORM

Analyse Structure of the conserved yeast listerin (Ltn1) N-terminal domain, MONOCLINIC… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5FG0
Type
protein
Length
814 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.41
Source
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Molecule
E3 ubiquitin-protein ligase listerin
EC
6.3.2.-
UniProt
Q04781
Ligands
K
Pockets
9 · best druggability 0.74

Structure

x-ray diffraction · resolution 2.41 · 1 distinct chain · 69% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BE3 ubiquitin-protein ligase listerin (EC 6.3.2.-)protein40769% helix, 0% strandQ04781

Ligands and binding sites

  • K · Potassium ion · metal · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15220.740.8242empty
28200.730.7870empty
32590.660.8324empty
42830.650.8124empty
51520.480.7718empty

Interfaces

1 interface between chains.

  • A–B · 725 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 5FG0 · Structure of the conserved yeast listerin (LTN1) N-terminal domain, monoclinic form · the same entry in another collection · chain A against A, TM-score 1.00
  • Q04781 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase listerin (Q04781) · a predicted model of the same protein · chain A against A, TM-score 0.97

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