GL1X · GenesisL1 explorer

Research workbench

Spore photoproduct lyase complexed with dinucleoside spore photoproduct

Analyse Spore photoproduct lyase complexed with dinucleoside spore photoproduct in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4FHD
Type
protein
Length
340 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Spore photoproduct lyase
UniProt
A4IQU1
Ligands
SF4, EEM, 0TT, POP, SO4
Pockets
4 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASpore photoproduct lyaseprotein34038% helix, 22% strandA4IQU1

Ligands and binding sites

  • SF4 · Iron/sulfur cluster · ligand · chains A
  • EEM · [(3S)-3-amino-4-hydroxy-4-oxo-butyl]-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methyl]-methyl-selanium · ligand · chains A
  • 0TT · 1-[(2R,4S,5R)-5-(hydroxymethyl)-4-oxidanyl-oxolan-2-yl]-5-[[(5R)-1-[(2R,4S,5R)-5-(hydroxymethyl)-4-oxidanyl-oxolan-2-yl]-5-methyl-2,4-bis(oxidanylidene)-1,3-diazinan-5-yl]methyl]pyrimidine-2,4-dione · ligand · chains A
  • POP · Pyrophosphate 2- · ligand · chains A
  • SO4 · Sulfate ion · ion · 5 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15480.780.8448SF4, EEM, 0TT, POP
2720.420.8120SO4
3790.350.7517empty
4640.320.7613empty

Compared structures

  • 4FHD · Spore photoproduct lyase complexed with dinucleoside spore photoproduct · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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