MolNFT v1 · #84216 · protein

Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955

3ZDR · Alcohol dehydrogenase domain of the bifunctional…: “Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus…”. X-ray diffraction, 2 ligands (ZN, SO4), 2 pockets (best druggability…

PDB: 3ZDR
Type: protein
Length: 403 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alcohol dehydrogenase domain of the bifunctional acetaldehyde dehydrogenase
EC: 1.2.1.10, 1.1.1.1
UniProt: F8CW95
Ligands: ZN, SO4
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alcohol dehydrogenase domain of the bifunctional acetaldehyde dehydrogenase (EC 1.2.1.10, 1.1.1.1)	protein	403	54% helix, 10% strand	F8CW95

Ligands and binding sites

ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	774	0.74	0.79	71	GOL
2	88	0.63	0.90	23	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

3ZDR · Structure of the Alcohol dehydrogenase (ADH) domain of a bifunctional ADHE dehydrogenase… · the same entry in another collection · chain A against A, TM-score 1.00

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 F8CW95
Elsewhere: RCSB PDB 3ZDR · PDBe 3ZDR · UniProt F8CW95

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