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Structures and transport dynamics of the campylobacter jejuni multidrug efflux pump cmeb

Analyse Structures and transport dynamics of the campylobacter jejuni multidrug efflux… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LQ3
Type: protein
Length: 6,202 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cmeb
UniProt: Q8RTE4
Pockets: 20 · best druggability 0.89

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E	Cmeb	protein	1033	51% helix, 17% strand	Q8RTE4
C, F	Cmeb	protein	1035	49% helix, 18% strand	Q8RTE4

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	992	0.89	0.91	128	empty
2	703	0.89	0.93	113	empty
3	501	0.87	0.94	82	empty
4	979	0.86	0.88	116	empty
5	934	0.86	0.88	116	empty

Interfaces

10 interfaces between chains.

D–E · 3539 Å² buried · 43 hydrogen bonds · protein-protein
A–B · 3535 Å² buried · 32 hydrogen bonds · protein-protein
A–C · 3447 Å² buried · 32 hydrogen bonds · protein-protein
E–F · 3440 Å² buried · 34 hydrogen bonds · protein-protein
B–C · 3410 Å² buried · 37 hydrogen bonds · protein-protein

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 Q8RTE4
Elsewhere: RCSB PDB 5LQ3 · PDBe 5LQ3 · UniProt Q8RTE4

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