Research workbench
Crystal structure of the C-terminal domain of HNUP98
Analyse Crystal structure of the C-terminal domain of HNUP98 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q5Y
- Type
- protein
- Length
- 306 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear pore complex protein NUP98; Nuclear pore complex protein NUP96
- UniProt
- P52948
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein NUP98 | protein | 152 | 20% helix, 34% strand | P52948 |
| B, D | Nuclear pore complex protein NUP96 | protein | 3 | 0% helix, 0% strand | P52948 |
| C | Nuclear pore complex protein NUP98 | protein | 148 | 18% helix, 35% strand | P52948 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.58 | 0.79 | 34 | empty |
| 2 | 66 | 0.45 | 0.82 | 14 | empty |
| 3 | 107 | 0.37 | 0.75 | 22 | empty |
Interfaces
4 interfaces between chains.
- A–C · 616 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 332 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 331 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 11 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2Q5Y · Crystal Structure of the C-terminal domain of hNup98 · 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 B 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 P52948
- Elsewhere: RCSB PDB 2Q5Y · PDBe 2Q5Y · UniProt P52948
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