GL1X · GenesisL1 explorer

Research workbench

Structure of a deoxyuridine 5'-triphosphate nucleotidohydrolase (dut) from coxiella burnetii

Analyse Structure of a deoxyuridine 5'-triphosphate nucleotidohydrolase (dut) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TQZ
Type
protein
Length
138 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Deoxyuridine 5'-triphosphate nucleotidohydrolase
EC
3.6.1.23
UniProt
Q45920
Ligands
SO4
Pockets
1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADeoxyuridine 5'-triphosphate nucleotidohydrolase (EC 3.6.1.23)protein1385% helix, 42% strandQ45920

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1750.380.7721empty

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

  • 3TQZ · Structure of a deoxyuridine 5'-triphosphate nucleotidohydrolase (dut) from Coxiella… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q45920 · AlphaFold monomer V2.0 prediction for deoxyuridine 5'-triphosphate nucleotidohydrolase… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.