MolNFT v1 · #106766 · protein
Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PEPT1 and PEPT2
4TPH · PROTON:OLIGOPEPTIDE symporter pot family: “Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PEPT1 and PEPT2”. X-ray diffraction, 1 ligand (ZN), 12 pockets (best druggability 0.78). MolNFT v1…
- PDB
- 4TPH
- Type
- protein
- Length
- 908 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PROTON:OLIGOPEPTIDE symporter pot family
- UniProt
- Q8EHE6
- Ligands
- ZN
- Pockets
- 12 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PROTON:OLIGOPEPTIDE symporter pot family | protein | 455 | 79% helix, 0% strand | Q8EHE6 |
| B | PROTON:OLIGOPEPTIDE symporter pot family | protein | 453 | 78% helix, 0% strand | Q8EHE6 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A, B
- LMT · Dodecyl-beta-D-maltoside · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1007 | 0.78 | 0.80 | 70 | empty |
| 2 | 742 | 0.76 | 0.81 | 55 | empty |
| 3 | 254 | 0.60 | 0.79 | 30 | empty |
| 4 | 277 | 0.59 | 0.78 | 34 | empty |
| 5 | 111 | 0.50 | 0.81 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 687 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 4TPH · Selectivity mechanism of a bacterial homologue of the human drug peptide transporters… · 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 Q8EHE6
- Elsewhere: RCSB PDB 4TPH · PDBe 4TPH · UniProt Q8EHE6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.