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Crystal structure of trypanosoma brucei N-acetyltransferase (TB11.01.2886) at 1.86A

Analyse Crystal structure of trypanosoma brucei N-acetyltransferase (TB11.01.2886) at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3I3G
Type
protein
Length
286 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-acetyltransferase
UniProt
Q383G8
Pockets
5 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BN-acetyltransferaseprotein14336% helix, 34% strandQ383G8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13720.680.8146empty
22560.610.8035empty
3570.320.7614empty
4730.300.7319empty
5680.290.7317empty

Interfaces

1 interface between chains.

  • A–B · 2957 Ų buried · 49 hydrogen bonds · protein-protein

Compared structures

  • 3I3G · Crystal Structure of Trypanosoma brucei N-acetyltransferase (Tb11.01.2886) at 1.86A · the same entry in another collection · chain A against A, TM-score 1.00

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