Research workbench

Horse liver alcohol dehydrogenase apo enzyme double mutant of gly 293 ala and pro 295 thr

Analyse Horse liver alcohol dehydrogenase apo enzyme double mutant of gly 293 ala and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QLJ
Type: protein
Length: 374 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alcohol dehydrogenase
EC: 1.1.1.1
UniProt: P00327
Ligands: ZN
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alcohol dehydrogenase (EC 1.1.1.1)	protein	374	30% 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	531	0.72	0.81	53	empty

Compared structures

1QLJ · Horse liver alcohol dehydrogenase apo enzyme double mutant of gly 293 ala and pro 295 thr · 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 0.98

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 1QLJ · PDBe 1QLJ · UniProt P00327

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