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Crystal structure of the nucleocapsid protein from bunyamwera virus bound to RNA
Analyse Crystal structure of the nucleocapsid protein from bunyamwera virus bound to RNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZLA
- Type
- protein + RNA
- Length
- 1,919 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein; RNA
- UniProt
- P16495
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 54% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, F, G, H | Nucleoprotein | protein | 229 | 54% helix, 9% strand | P16495 |
| D | Nucleoprotein | protein | 228 | 54% helix, 9% strand | P16495 |
| I, J | RNA | rna | 44 | — | — |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.84 | 0.95 | 41 | empty |
| 2 | 328 | 0.84 | 0.94 | 40 | empty |
| 3 | 311 | 0.84 | 0.94 | 39 | empty |
| 4 | 330 | 0.84 | 0.94 | 41 | empty |
| 5 | 317 | 0.84 | 0.94 | 41 | empty |
Interfaces
24 interfaces between chains.
- B–I · 1442 Ų buried · 26 hydrogen bonds · protein-nucleic
- G–J · 1395 Ų buried · 23 hydrogen bonds · protein-nucleic
- E–J · 1382 Ų buried · 19 hydrogen bonds · protein-nucleic
- F–J · 1380 Ų buried · 20 hydrogen bonds · protein-nucleic
- D–I · 1368 Ų buried · 19 hydrogen bonds · protein-nucleic
Compared structures
- 3ZLA · Crystal structure of the nucleocapsid protein from Bunyamwera virus bound to RNA · 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 P16495
- Elsewhere: RCSB PDB 3ZLA · PDBe 3ZLA · UniProt P16495
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