Research workbench

Structure of the 2,4'-dihydroxyacetophenone dioxygenase from alcaligenes sp. 4HAP.

Analyse Structure of the 2,4'-dihydroxyacetophenone dioxygenase from alcaligenes sp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5BPX
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2,4'-dihydroxyacetophenone dioxygenase
EC: 1.13.11.41
UniProt: Q9REI7
Ligands: FE
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2,4'-dihydroxyacetophenone dioxygenase (EC 1.13.11.41)	protein	153	15% helix, 42% strand	Q9REI7

Ligands and binding sites

FE · Fe (III) ion · metal · chains A
ACT · Acetate ion · additive · chains A
GOL · Glycerol · additive · 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	81	0.79	0.99	19	ACT, GOL

Compared structures

5BPX · Structure of the 2,4'-dihydroxyacetophe dioxygenase from Alcaligenes sp. 4HAP. · 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 Q9REI7
Elsewhere: RCSB PDB 5BPX · PDBe 5BPX · UniProt Q9REI7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.