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Crystallographic snapshots of aspergillus fumigatus phytase revealing its enzymatic dynamics

Analyse Crystallographic snapshots of aspergillus fumigatus phytase revealing its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SKA
Type
protein
Length
435 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
3-phytase a
EC
3.1.3.8
UniProt
O00092
Ligands
NAG
Pockets
2 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A3-phytase a (EC 3.1.3.8)protein43543% helix, 12% strandO00092

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13630.580.7644empty
21140.400.7523empty

Modifications

Observed in the structure: 5 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

  • 1SKA · Crystallographic snapshots of Aspergillus fumigatus phytase revealing its enzymatic… · the same entry in another collection · chain A against A, TM-score 1.00
  • O00092 · AlphaFold monomer V2.0 prediction for 3-phytase a (O00092) · a predicted model of the same protein · chain A against A, TM-score 1.00

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