MolNFT v1 · #91118 · protein
Crystal structure of periplasmic D-alanine ABC transporter from salmonella enterica
4F3S · Putative periplasmic binding protein: “Crystal structure of periplasmic D-alanine ABC transporter from salmonella enterica”. X-ray diffraction, 3 ligands (GLY, DAL, PO4), 1 pocket (best druggability 0.29). MolNFT v1 #91118 on…
- PDB
- 4F3S
- Type
- protein
- Length
- 231 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative periplasmic binding protein
- UniProt
- Q8ZPA3
- Ligands
- GLY, DAL, PO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative periplasmic binding protein | protein | 231 | 39% helix, 29% strand | Q8ZPA3 |
Ligands and binding sites
- GLY · Glycine · ligand · chains A
- DAL · D-alanine · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.29 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 4F3S · Crystal structure of periplasmic D-alanine ABC transporter from Salmonella enterica · 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 Q8ZPA3
- Elsewhere: RCSB PDB 4F3S · PDBe 4F3S · UniProt Q8ZPA3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.