MolNFT v1 · #22597 · protein

Structural basis of multidrug transport by the acrb multidrug efflux pump

1T9V · Acriflavine resistance protein B: “Structural basis of multidrug transport by the acrb multidrug efflux pump”. X-ray diffraction, 1 ligand (RHQ), 10 pockets (best druggability 0.86). MolNFT v1 #22597 on GenesisL1: 3D structure…

PDB: 1T9V
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: RHQ
Pockets: 10 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acriflavine resistance protein B	protein	1014	44% helix, 15% strand	P31224

Ligands and binding sites

RHQ · Rhodamine 6G · ligand · 2 copies · chains A

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

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1012	0.86	0.87	117	empty
2	52	0.68	0.96	18	empty
3	199	0.65	0.85	33	empty
4	383	0.64	0.78	52	empty
5	289	0.58	0.77	39	empty

Compared structures

1T9V · 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 1T9V · PDBe 1T9V · UniProt P31224

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