MolNFT v1 · #130960 · protein
E1M, Y96W, S119W mutant of rh. blastica porin
5PRN: “E1M, Y96W, S119W mutant of rh. blastica porin”. X-ray diffraction, 3 pockets (best druggability 0.44). MolNFT v1 #130960 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5PRN
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Porin
- UniProt
- P39767
- Pockets
- 3 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Porin | protein | 289 | 4% helix, 55% strand | P39767 |
Ligands and binding sites
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.44 | 0.73 | 39 | empty |
| 2 | 81 | 0.34 | 0.75 | 17 | empty |
| 3 | 71 | 0.32 | 0.75 | 17 | empty |
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 P39767
- Elsewhere: RCSB PDB 5PRN · PDBe 5PRN · UniProt P39767
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