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The crystal structure of a universal stress protein E from proteus mirabilis HI4320

Analyse The crystal structure of a universal stress protein E from proteus mirabilis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OLQ
Type
protein
Length
306 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Universal stress protein E
UniProt
B4ETT2
Ligands
UNL
Pockets
5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUniversal stress protein Eprotein30644% helix, 20% strandB4ETT2

Ligands and binding sites

  • UNL · Unknown ligand · ligand · chains A
  • GOL · Glycerol · additive · 2 copies · chains A
  • PEG · Di(hydroxyethyl)ether · additive · chains A
  • ACT · Acetate ion · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11860.700.8833GOL
21380.630.8623empty
3900.460.8022empty
4500.300.7617empty
5790.290.7219empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 3OLQ · The crystal structure of a universal stress protein E from Proteus mirabilis HI4320 · the same entry in another collection · chain A against A, TM-score 1.00

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