GL1X · GenesisL1 explorer

Research workbench

Crystal structure of acinetobacter sp. DL28 L-ribose isomerase mutant E204Q in complex with L-ribose

Analyse Crystal structure of acinetobacter sp. DL28 L-ribose isomerase mutant E204Q in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4Q0U
Type
protein
Length
249 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-ribose isomerase
EC
5.3.1.-
UniProt
Q93UQ5
Ligands
Z6J, ROR, NCO, 0MK, CO
Pockets
3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AL-ribose isomerase (EC 5.3.1.-)protein24917% helix, 27% strandQ93UQ5

Ligands and binding sites

  • Z6J · alpha-L-ribofuranose · ligand · 3 copies · chains A
  • ROR · L-ribose · ligand · chains A
  • NCO · Cobalt hexammine(iii) · ligand · chains A
  • 0MK · beta-L-ribopyranose · sugar · chains A
  • CO · Cobalt (II) ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12460.630.8234empty
2910.330.7314empty
3500.270.7413empty

Compared structures

  • 4Q0U · Crystal structure of Acinetobacter sp. DL28 L-ribose isomerase mutant E204Q in complex… · 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.