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The crystal structure of the acetyltransferase from enterococcus faecalis

Analyse The crystal structure of the acetyltransferase from enterococcus faecalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FIA
Type
protein
Length
316 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acetyltransferase
Pockets
3 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetyltransferaseprotein15736% helix, 31% strand—
BAcetyltransferaseprotein15938% helix, 26% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11220.720.9230empty
21010.690.9225empty
3560.300.7517empty

Interfaces

1 interface between chains.

  • A–B · 693 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 2FIA · The crystal structure of the acetyltransferase from Enterococcus faecalis · the same entry in another collection · chain A against A, TM-score 1.00

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