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Structure of conserved protein of unknown function EF2215 from enterococcus faecalis

Analyse Structure of conserved protein of unknown function EF2215 from enterococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NN5
Type
protein
Length
171 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein EF_2215
UniProt
Q832L1
Ligands
MG
Pockets
1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypothetical protein EF_2215protein17135% helix, 37% strandQ832L1

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A
  • EDO · 1,2-ethanediol · additive · 2 copies · 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
11430.430.7523empty

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

  • 2NN5 · Structure of Conserved Protein of Unknown Function EF2215 from Enterococcus faecalis · the same entry in another collection · chain A against A, TM-score 1.00

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