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Substrate and cofactor-free form of the aldehyde reductase yqhd from E. COLI.

Analyse Substrate and cofactor-free form of the aldehyde reductase yqhd from E. COLI. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QGS
Type: protein
Length: 380 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alcohol dehydrogenase yqhd
EC: 1.1.1.-
UniProt: Q46856
Ligands: ZN, CL
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alcohol dehydrogenase yqhd (EC 1.1.1.-)	protein	380	50% helix, 10% strand	Q46856

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · 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	1088	0.74	0.77	91	empty

Compared structures

4QGS · Substrate and cofactor-free form of the Aldehyde Reductase YqhD from E. coli. · the same entry in another collection · chain A against A, TM-score 1.00
Q46856 · AlphaFold monomer V2.0 prediction for alcohol dehydrogenase yqhd (Q46856) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q46856
Elsewhere: RCSB PDB 4QGS · PDBe 4QGS · UniProt Q46856

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