Research workbench
Crystal structure of E.coli MacA
Analyse Crystal structure of E.coli MacA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FPP
- Type
- protein
- Length
- 533 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.99
- Source
- Escherichia coli
- Molecule
- Macrolide-specific efflux protein macA
- UniProt
- P75830
- Pockets
- 5 · best druggability 0.56
Structure
x-ray diffraction · resolution 2.99 · 2 distinct chains · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrolide-specific efflux protein macA | protein | 266 | 28% helix, 27% strand | P75830 |
| B | Macrolide-specific efflux protein macA | protein | 267 | 30% helix, 30% strand | P75830 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.56 | 0.83 | 19 | empty |
| 2 | 330 | 0.54 | 0.74 | 32 | empty |
| 3 | 185 | 0.52 | 0.78 | 29 | empty |
| 4 | 91 | 0.35 | 0.75 | 23 | empty |
| 5 | 68 | 0.29 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2011 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
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 P75830
- Elsewhere: RCSB PDB 3FPP · PDBe 3FPP · UniProt P75830
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.