MolNFT v1 · #24553 · protein
Translocator domain of autotransporter nalp from neisseria meningitidis
1UYO: “Translocator domain of autotransporter nalp from neisseria meningitidis”. X-ray diffraction, 1 ligand (CXE), 3 pockets (best druggability 0.85). MolNFT v1 #24553 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1UYO
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nalp
- UniProt
- Q8GKS5
- Ligands
- CXE
- Pockets
- 3 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 68% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Nalp | protein | 277 | 9% helix, 68% strand | Q8GKS5 |
Ligands and binding sites
- CXE · Pentaethylene glycol monodecyl ether · ligand · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 673 | 0.85 | 0.90 | 78 | empty |
| 2 | 74 | 0.72 | 0.97 | 28 | empty |
| 3 | 219 | 0.56 | 0.79 | 32 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 1UYO · Translocator domain of autotransporter NalP from Neisseria meningitidis · the same entry in another collection · chain X against X, 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 Q8GKS5
- Elsewhere: RCSB PDB 1UYO · PDBe 1UYO · UniProt Q8GKS5
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