MolNFT v1 · #17597 · protein

Structural basis of multiple binding capacity of the acrb multidrug efflux pump

1OYD · Acriflavine resistance protein B: “Structural basis of multiple binding capacity of the acrb multidrug efflux pump”. X-ray diffraction, 1 ligand (DEQ), 14 pockets (best druggability 0.79). MolNFT v1 #17597 on GenesisL1: 3D…

PDB: 1OYD
Type: protein
Length: 1,006 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acriflavine resistance protein B
UniProt: P31224
Ligands: DEQ
Pockets: 14 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acriflavine resistance protein B	protein	1006	46% helix, 15% strand	P31224

Ligands and binding sites

DEQ · Dequalinium · ligand · chains A

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

Pockets

14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	394	0.79	0.88	42	empty
2	317	0.73	0.86	51	empty
3	57	0.70	0.96	14	empty
4	51	0.66	0.96	25	empty
5	263	0.59	0.78	34	empty

Compared structures

1OYD · Structural Basis of Multiple Binding Capacity of the AcrB multidrug Efflux Pump · the same entry in another collection · chain A against A, TM-score 1.00
P31224 · AlphaFold monomer V2.0 prediction for multidrug efflux pump subunit acrb (P31224) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P31224
Elsewhere: RCSB PDB 1OYD · PDBe 1OYD · UniProt P31224

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