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Interdomain motion in liver alcohol dehydrogenase. structural and energetic analysis of the hinge bending mode

Analyse Interdomain motion in liver alcohol dehydrogenase. structural and energetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ADH
Type
protein
Length
374 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Apo-liver alcohol dehydrogenase
EC
1.1.1.1
UniProt
P00327
Ligands
APR, ZN
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AApo-liver alcohol dehydrogenase (EC 1.1.1.1)protein37426% helix, 25% strandP00327

Ligands and binding sites

  • APR · Adenosine-5-diphosphoribose · ligand · chains A
  • ZN · Zinc ion · metal · 2 copies · chains A
  • MPD · (4S)-2-methyl-2,4-pentanediol · additive · 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
16190.730.8056APR, MPD

Compared structures

  • 5ADH · Interdomain motion in liver alcohol dehydrogenase. structural and energetic analysis of… · the same entry in another collection · chain A against A, TM-score 1.00
  • P00327 · AlphaFold monomer V2.0 prediction for alcohol dehydrogenase E chain (P00327) · a predicted model of the same protein · chain A against A, TM-score 0.97

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