Research workbench

Alcohol dehydrogenase from thauera aromatica K319A/K320A mutant

Analyse Alcohol dehydrogenase from thauera aromatica K319A/K320A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QUL
Type: protein
Length: 351 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase
EC: 1.1.1.368
UniProt: O87871
Ligands: ZN
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase (EC 1.1.1.368)	protein	351	33% helix, 24% strand	O87871

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 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	729	0.74	0.79	77	EDO

Compared structures

7QUL · Alcohol Dehydrogenase from Thauera aromatica K319A/K320A mutant · the same entry in another collection · chain A against A, TM-score 1.00
O87871 · AlphaFold monomer V2.0 prediction for 6-hydroxycyclohex-1-ene-1-carbonyl-CoA… · 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 O87871
Elsewhere: RCSB PDB 7QUL · PDBe 7QUL · UniProt O87871

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