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Cryo-EM structures of adeb from acinetobacter baumannii: adeb-III

Analyse Cryo-EM structures of adeb from acinetobacter baumannii: adeb-III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KGF
Type: protein
Length: 3,060 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Efflux pump membrane transporter
UniProt: Q2FD70
Pockets: 20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 55% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Efflux pump membrane transporter	protein	1020	55% helix, 19% strand	Q2FD70

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	913	0.88	0.90	124	empty
2	1036	0.87	0.88	141	empty
3	1069	0.87	0.88	143	empty
4	816	0.83	0.85	41	empty
5	565	0.74	0.82	62	empty

Interfaces

3 interfaces between chains.

A–C · 2109 Å² buried · 22 hydrogen bonds · protein-protein
A–B · 2100 Å² buried · 22 hydrogen bonds · protein-protein
B–C · 2099 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

7KGF · Cryo-EM Structures of AdeB from Acinetobacter baumannii: AdeB-III · 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 Q2FD70
Elsewhere: RCSB PDB 7KGF · PDBe 7KGF · UniProt Q2FD70

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