Research workbench
Crystal structure of C-terminal autoproteolytic domain of nucleoporin NUP98
Analyse Crystal structure of C-terminal autoproteolytic domain of nucleoporin NUP98 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KO6
- Type
- protein
- Length
- 312 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear pore complex protein NUP98
- UniProt
- P52948
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 3 distinct chains · 21% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein NUP98 | protein | 152 | 21% helix, 30% strand | P52948 |
| B, D | Nuclear pore complex protein NUP98 | protein | 6 | 0% helix, 33% strand | P52948 |
| C | Nuclear pore complex protein NUP98 | protein | 148 | 21% helix, 28% strand | P52948 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.60 | 0.76 | 53 | empty |
Interfaces
4 interfaces between chains.
- A–C · 654 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 476 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 460 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 126 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1KO6 · Crystal Structure of C-terminal Autoproteolytic Domain of Nucleoporin Nup98 · the same entry in another collection · chain A against A, TM-score 1.00
- P52948 · AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP98-NUP96 (P52948) · a predicted model of the same protein · chain C against A, TM-score 0.98
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 P52948
- Elsewhere: RCSB PDB 1KO6 · PDBe 1KO6 · UniProt P52948
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.