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Crystal structure of mouse cytosolic sulfotransferase MSULT1D1 complex with paps

Analyse Crystal structure of mouse cytosolic sulfotransferase MSULT1D1 complex with paps in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZYT
Type
protein
Length
291 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine-ester sulfotransferase
EC
2.8.2.9
UniProt
Q9R2C2
Ligands
PPS
Pockets
1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
XTyrosine-ester sulfotransferase (EC 2.8.2.9)protein29144% helix, 11% strandQ9R2C2

Ligands and binding sites

  • PPS · 3'-phosphate-adenosine-5'-phosphate sulfate · ligand · chains X
  • GOL · Glycerol · additive · 2 copies · chains X

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
13020.820.9259PPS

Compared structures

  • 2ZYT · Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAPS · the same entry in another collection · chain X against X, TM-score 1.00

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