Research workbench
Cryo-EM structures of adeb from acinetobacter baumannii: adeb-et-I
Analyse Cryo-EM structures of adeb from acinetobacter baumannii: adeb-et-I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KGG
- 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
- Ligands
- PTY, ET
- Pockets
- 20 · best druggability 0.85
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 |
Ligands and binding sites
- PTY · Phosphatidylethanolamine · ligand · 6 copies · chains A, B, C
- ET · Ethidium · ligand · 3 copies · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1200 | 0.85 | 0.86 | 135 | empty |
| 2 | 631 | 0.84 | 0.89 | 77 | empty |
| 3 | 778 | 0.83 | 0.86 | 85 | empty |
| 4 | 404 | 0.82 | 0.90 | 50 | empty |
| 5 | 734 | 0.78 | 0.83 | 79 | empty |
Interfaces
3 interfaces between chains.
- A–C · 3397 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 3091 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 2940 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 7KGG · Cryo-EM Structures of AdeB from Acinetobacter baumannii: AdeB-ET-I · 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 7KGG · PDBe 7KGG · UniProt Q2FD70
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