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Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product

Analyse Crystal structure of the CTP1L endolysin reveals how its activity is regulated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5A6S
Type
protein
Length
352 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endolysin
UniProt
D9ZNF3
Ligands
SO4
Pockets
3 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndolysinprotein27334% helix, 26% strandD9ZNF3
BEndolysinprotein7937% helix, 20% strandD9ZNF3

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A
  • GOL · Glycerol · additive · 3 copies · chains A, B
  • 1PE · Pentaethylene glycol · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13560.630.7834empty
2640.370.7816empty
3790.350.7619SO4

Interfaces

1 interface between chains.

  • A–B · 801 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 5A6S · Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a… · the same entry in another collection · chain A against A, TM-score 1.00

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