GL1X · GenesisL1 explorer

Research workbench

Crystal structure of 2-dehydropantoate 2-reductase from porphyromonas gingivalis W83

Analyse Crystal structure of 2-dehydropantoate 2-reductase from porphyromonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QYT
Type
protein
Length
287 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
2-dehydropantoate 2-reductase
UniProt
Q7MT04
Ligands
SO4
Pockets
3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A2-dehydropantoate 2-reductaseprotein28746% helix, 23% strandQ7MT04

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 5 copies · chains A
  • EDO · 1,2-ethanediol · additive · 5 copies · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1690.540.8627empty
22950.530.7536SO4, EDO
31680.440.7422empty

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 2QYT · Crystal structure of 2-dehydropantoate 2-reductase from Porphyromonas gingivalis W83 · 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.