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Acinetobacter baumannii multidrug transporter adeb in L*OO state

Analyse Acinetobacter baumannii multidrug transporter adeb in L*OO state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7B8Q
Type: protein
Length: 3,041 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Efflux pump membrane transporter
UniProt: B0V4F5
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 2 distinct chains · 53% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Efflux pump membrane transporter	protein	1011	53% helix, 18% strand	B0V4F5
B, C	Efflux pump membrane transporter	protein	1015	52% helix, 17% strand	B0V4F5

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	969	0.87	0.89	118	empty
2	747	0.84	0.88	107	empty
3	547	0.84	0.90	74	empty
4	196	0.77	0.93	35	empty
5	407	0.76	0.86	36	empty

Interfaces

3 interfaces between chains.

A–B · 3482 Å² buried · 35 hydrogen bonds · protein-protein
B–C · 3172 Å² buried · 31 hydrogen bonds · protein-protein
A–C · 3008 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

7B8Q · Acinetobacter baumannii multidrug transporter AdeB in L*OO state · 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 B0V4F5
Elsewhere: RCSB PDB 7B8Q · PDBe 7B8Q · UniProt B0V4F5

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