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Crystal structure of a deoxyuridine 5'-triphosphate nucleotidohydrolase from burkholderia thailandensis

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

PDB
4LHR
Type
protein
Length
134 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
Q2T0H6
Pockets
2 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADeoxyuridine 5'-triphosphate nucleotidohydrolase (EC 3.6.1.23)protein1349% helix, 41% strandQ2T0H6

Ligands and binding sites

  • PG4 · Tetraethylene glycol · additive · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.390.8013empty
2500.240.7212empty

Compared structures

  • 4LHR · Crystal structure of a deoxyuridine 5'-triphosphate nucleotidohydrolase from Burkholderia… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q2T0H6 · AlphaFold monomer V2.0 prediction for deoxyuridine 5'-triphosphate nucleotidohydrolase… · a predicted model of the same protein · chain A against A, TM-score 0.97

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