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2.6 ångström crystal structure of putative yceg-like protein LMO1499 from listeria monocytogenes

Analyse 2.6 ångström crystal structure of putative yceg-like protein LMO1499 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4IIW
Type
protein
Length
611 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LMO1499 protein
UniProt
Q8Y725
Ligands
CL, SO4
Pockets
8 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALMO1499 proteinprotein30445% helix, 8% strandQ8Y725
BLMO1499 proteinprotein30746% helix, 7% strandQ8Y725

Ligands and binding sites

  • CL · Chloride ion · ion · 6 copies · chains A, B
  • SO4 · Sulfate ion · ion · 6 copies · chains A, B
  • PGE · Triethylene glycol · additive · chains A

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

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11120.580.8528empty
23310.580.7644empty
32780.580.7831empty
41910.500.7627empty
52360.490.7425empty

Interfaces

1 interface between chains.

  • A–B · 710 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

  • 4IIW · 2.6 Angstrom Crystal Structure of Putative yceG-like Protein lmo1499 from Listeria… · the same entry in another collection · chain A against A, TM-score 1.00

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