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Crystal structure of putative N-acetyltransferase from lactobacillus plantarum

Analyse Crystal structure of putative N-acetyltransferase from lactobacillus plantarum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EFA
Type
protein
Length
146 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative acetyltransferase
UniProt
Q88W61
Ligands
PO4
Pockets
1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative acetyltransferaseprotein14634% helix, 35% strandQ88W61

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A
  • FMT · Formic acid · additive · 4 copies · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15150.670.7842FMT, GOL

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

  • 3EFA · Crystal structure of putative N-acetyltransferase from Lactobacillus plantarum · the same entry in another collection · chain A against A, TM-score 1.00

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