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NMR structure of a 180 residue construct encompassing the N-terminal metal-binding site and the membrane proximal domain of silb from cupriavidus metallidurans CH34
Analyse NMR structure of a 180 residue construct encompassing the N-terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A4G
- Type
- protein
- Length
- 180 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Silb, silver efflux protein, mfp component of the three components proton antiporter…
- UniProt
- Q58AF3
- Ligands
- AG
- Pockets
- 2 · best druggability 0.57
Structure
solution nmr · 1 distinct chain · 2% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Silb, silver efflux protein, mfp component of the three components proton antiporter metal efflux system | protein | 180 | 2% helix, 28% strand | Q58AF3 |
Ligands and binding sites
- AG · Silver ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 327 | 0.57 | 0.76 | 39 | empty |
| 2 | 91 | 0.33 | 0.73 | 19 | empty |
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 Q58AF3
- Elsewhere: RCSB PDB 5A4G · PDBe 5A4G · UniProt Q58AF3
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