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The crystal structure of a putative hemolysin from lactococcus lactis

Analyse The crystal structure of a putative hemolysin from lactococcus lactis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OPN
Type
protein
Length
208 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative hemolysin
UniProt
Q9CH80
Ligands
SO4
Pockets
1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative hemolysinprotein20835% helix, 20% strandQ9CH80

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A
  • GOL · Glycerol · additive · 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
11700.480.7736SO4

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

  • 3OPN · The crystal structure of a putative hemolysin from Lactococcus lactis · the same entry in another collection · chain A against A, TM-score 1.00

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