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Crystal structure of the nipah virus phosphoprotein multimerization domain G519N
Analyse Crystal structure of the nipah virus phosphoprotein multimerization domain G519N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EB8
- Type
- protein
- Length
- 811 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoprotein
- UniProt
- Q9IK91
- Pockets
- 8 · best druggability 0.69
Structure
x-ray diffraction · 5 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoprotein | protein | 104 | 83% helix, 0% strand | Q9IK91 |
| E | Phosphoprotein | protein | 103 | 87% helix, 0% strand | Q9IK91 |
| D, H, F, G | Phosphoprotein | protein | 101 | 83% helix, 0% strand | Q9IK91 |
| C | Phosphoprotein | protein | 100 | 81% helix, 0% strand | Q9IK91 |
| B | Phosphoprotein | protein | 100 | 80% helix, 0% strand | Q9IK91 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 836 | 0.69 | 0.75 | 69 | empty |
| 2 | 117 | 0.44 | 0.77 | 18 | empty |
| 3 | 93 | 0.40 | 0.77 | 13 | empty |
| 4 | 74 | 0.39 | 0.78 | 13 | empty |
| 5 | 79 | 0.39 | 0.78 | 13 | empty |
Interfaces
15 interfaces between chains.
- E–F · 2636 Ų buried · 27 hydrogen bonds · protein-protein
- D–C · 2598 Ų buried · 25 hydrogen bonds · protein-protein
- H–G · 2590 Ų buried · 34 hydrogen bonds · protein-protein
- A–B · 2563 Ų buried · 26 hydrogen bonds · protein-protein
- A–D · 2502 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 6EB8 · Crystal Structure of the Nipah Virus Phosphoprotein Multimerization Domain G519N · the same entry in another collection · chain A 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 Q9IK91
- Elsewhere: RCSB PDB 6EB8 · PDBe 6EB8 · UniProt Q9IK91
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