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Crystal structure of GCN5-related N-acetyltransferase from sphaerobacter thermophilus

Analyse Crystal structure of GCN5-related N-acetyltransferase from sphaerobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TT2
Type
protein
Length
315 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GCN5-related N-acetyltransferase
UniProt
D1C2H7
Ligands
SO4
Pockets
3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGCN5-related N-acetyltransferaseprotein31533% helix, 32% strandD1C2H7

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 6 copies · chains A
  • GOL · Glycerol · additive · 5 copies · chains A
  • MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16790.760.8158GOL, SO4, MES
21400.470.7720empty
3920.340.7424SO4

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 3TT2 · Crystal Structure of GCN5-related N-Acetyltransferase from Sphaerobacter thermophilus · the same entry in another collection · chain A against A, TM-score 1.00

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