Research workbench

Conformation of the acrb multidrug efflux pump in mutants of the putative proton relay pathway

Analyse Conformation of the acrb multidrug efflux pump in mutants of the putative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HQD
Type: protein
Length: 1,016 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acriflavine resistance protein B
UniProt: P31224
Pockets: 15 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acriflavine resistance protein B	protein	1016	34% helix, 15% strand	P31224

Pockets

15 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	1133	0.85	0.86	98	empty
2	155	0.78	0.94	28	empty
3	53	0.73	0.99	17	empty
4	52	0.71	0.98	23	empty
5	389	0.63	0.78	49	empty

Compared structures

2HQD · Conformation of the AcrB Multidrug Efflux Pump in Mutants of the Putative Proton Relay… · 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 2HQD · PDBe 2HQD · UniProt P31224

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