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Crystal structure of human glucosamine 6-phosphate N-acetyltransferase 1 mutant E156A

Analyse Crystal structure of human glucosamine 6-phosphate N-acetyltransferase 1 mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CXP
Type
protein
Length
184 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glucosamine 6-phosphate N-acetyltransferase
EC
2.3.1.4
UniProt
Q96EK6
Ligands
CL
Pockets
3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlucosamine 6-phosphate N-acetyltransferase (EC 2.3.1.4)protein18433% helix, 23% strandQ96EK6

Ligands and binding sites

  • CL · Chloride ion · ion · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11370.480.7822empty
21320.440.7619empty
3860.320.7315empty

Compared structures

  • 3CXP · Crystal structure of human glucosamine 6-phosphate N-acetyltransferase 1 mutant E156A · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96EK6 · AlphaFold monomer V2.0 prediction for glucosamine 6-phosphate N-acetyltransferase (Q96EK6) · a predicted model of the same protein · chain A against A, TM-score 1.00

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