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Structural basis of multidrug transport by the acrb multidrug efflux pump

Analyse Structural basis of multidrug transport by the acrb multidrug efflux pump in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T9X
Type: protein
Length: 1,014 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acriflavine resistance protein B
UniProt: P31224
Ligands: ET
Pockets: 8 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acriflavine resistance protein B	protein	1014	43% helix, 16% strand	P31224

Ligands and binding sites

ET · Ethidium · ligand · 2 copies · chains A

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

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	977	0.87	0.88	120	empty
2	55	0.64	0.94	19	empty
3	163	0.62	0.85	25	empty
4	111	0.59	0.86	23	empty
5	279	0.58	0.78	32	empty

Compared structures

1T9X · Structural Basis of Multidrug Transport by 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 1T9X · PDBe 1T9X · UniProt P31224

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