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Crystal structure of a putative efflux transporter (BACEGG_01895) from bacteroides eggerthii dsm 20697 at 2.06 a resolution

Analyse Crystal structure of a putative efflux transporter (BACEGG_01895) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L8J
Type: protein
Length: 326 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative efflux transporter
UniProt: B7AHL2
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative efflux transporter	protein	326	23% helix, 32% strand	B7AHL2

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	258	0.50	0.74	45	empty
2	112	0.40	0.76	19	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

4L8J · Crystal structure of a Putative efflux transporter (BACEGG_01895) from Bacteroides… · 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 B7AHL2
Elsewhere: RCSB PDB 4L8J · PDBe 4L8J · UniProt B7AHL2

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