GL1X · GenesisL1 explorer

Research workbench

Structure of HIS387ALA mutant of the propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment

Analyse Structure of HIS387ALA mutant of the propionaldehyde dehydrogenase from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DRU
Type
protein
Length
435 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aldehyde dehydrogenase
UniProt
A9KN57
Ligands
SO4
Pockets
1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAldehyde dehydrogenaseprotein43545% helix, 21% strandA9KN57

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13230.650.8048empty

Compared structures

  • 5DRU · Structure of His387Ala mutant of the propionaldehyde dehydrogenase from the Clostridium… · 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.