GL1X · GenesisL1 explorer

Research workbench

AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase (P31867)

Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P31867
Type
protein
Length
318 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xeD1A6159e26791F22a6cE039130D208Ac313c418
Molecule
NAD(P)H-dependent D-xylose reductase
UniProt
P31867
Pockets
1 · best druggability 0.71

Structure

1 distinct chain · 41% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANAD(P)H-dependent D-xylose reductaseprotein31841% helix, 15% strandP31867

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13390.710.8343empty

Compared structures

  • 5Z6T · Crystal structure of D-xylose reductase from scheffersomyces stipitis in complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.99
  • 5Z6T · Crystal structure of D-xylose reductase from Scheffersomyces stipitis in complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.99
  • 5Z6U · Crystal structure of D-xylose reductase from scheffersomyces stipitis · an experimental structure of the same protein · chain A against A, TM-score 0.98
  • 5Z6U · Crystal structure of D-xylose reductase from Scheffersomyces stipitis · an experimental structure of the same protein · chain A against A, TM-score 0.98

Analyse

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