GL1X · GenesisL1 explorer

Research workbench

Structure of uracil phosphoribosyl transferase

Analyse Structure of uracil phosphoribosyl transferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2EHJ
Type
protein
Length
832 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uracil phosphoribosyltransferase
EC
2.4.2.9
UniProt
P0A8F0
Ligands
SO4
Pockets
14 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DUracil phosphoribosyltransferase (EC 2.4.2.9)protein20835% helix, 32% strandP0A8F0

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 19 copies · chains A, B, C, D

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

Pockets

14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19550.890.9095empty
22930.750.8831SO4
34020.750.8536SO4
42980.740.8733SO4
53270.720.8532SO4

Interfaces

6 interfaces between chains.

  • A–D · 1890 Ų buried · 18 hydrogen bonds · protein-protein
  • B–C · 1820 Ų buried · 19 hydrogen bonds · protein-protein
  • C–D · 1095 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 1072 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 116 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 2EHJ · Structure of Uracil phosphoribosyl transferase · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A8F0 · AlphaFold monomer V2.0 prediction for uracil phosphoribosyltransferase (P0A8F0) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

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