Research workbench
Crystal structure of the N-terminal domain of NUP159
Analyse Crystal structure of the N-terminal domain of NUP159 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XIP
- Type
- protein
- Length
- 367 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoporin NUP159
- UniProt
- P40477
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoporin NUP159 | protein | 367 | 4% helix, 53% strand | P40477 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 373 | 0.64 | 0.79 | 36 | empty |
| 2 | 65 | 0.46 | 0.83 | 18 | empty |
| 3 | 111 | 0.45 | 0.78 | 18 | empty |
| 4 | 65 | 0.38 | 0.79 | 14 | empty |
Modifications
Observed in the structure: 3 modified (engineered).
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 P40477
- Elsewhere: RCSB PDB 1XIP · PDBe 1XIP · UniProt P40477
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.