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Crystal structure of glucosamine-6-phosphate N-acetyltransferase from arabidopsis thaliana

Analyse Crystal structure of glucosamine-6-phosphate N-acetyltransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3T90
Type
protein
Length
147 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glucose-6-phosphate acetyltransferase 1
UniProt
Q9LFU9
Ligands
NA
Pockets
3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlucose-6-phosphate acetyltransferase 1protein14737% helix, 26% strandQ9LFU9

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 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
12500.560.7729empty
21280.440.7717empty
31340.420.7523EPE

Compared structures

  • 3T90 · Crystal structure of glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9LFU9 · AlphaFold monomer V2.0 prediction for glucosamine 6-phosphate N-acetyltransferase (Q9LFU9) · a predicted model of the same protein · chain A against A, TM-score 0.98

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