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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: 8ADH
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: ZN
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apo-liver alcohol dehydrogenase (EC 1.1.1.1)	protein	374	29% helix, 24% strand	P00327

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	512	0.73	0.82	53	empty

Compared structures

8ADH · 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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00327
Elsewhere: RCSB PDB 8ADH · PDBe 8ADH · UniProt P00327

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