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Crystal structures of SULT1A2 and SULT1A1*3: implications in the bioactivation of N-hydroxy-2-acetylamino fluorine (oh-aaf)

Analyse Crystal structures of SULT1A2 and SULT1A1*3: implications in the bioactivation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Z29
Type
protein
Length
281 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenol-sulfating phenol sulfotransferase 2
EC
2.8.2.1
UniProt
P50226
Ligands
A3P, CA
Pockets
1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhenol-sulfating phenol sulfotransferase 2 (EC 2.8.2.1)protein28142% helix, 11% strandP50226

Ligands and binding sites

  • A3P · Adenosine-3'-5'-diphosphate · ligand · chains A
  • CA · Calcium ion · metal · chains A
  • ACY · Acetic acid · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13230.830.9357CA, A3P, ACY

Compared structures

  • 1Z29 · Crystal Structures of SULT1A2 and SULT1A1*3: Implications in the bioactivation of… · the same entry in another collection · chain A against A, TM-score 1.00
  • P50226 · AlphaFold monomer V2.0 prediction for sulfotransferase 1A2 (P50226) · a predicted model of the same protein · chain A against A, TM-score 1.00

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