Research workbench
N-terminal globular domain of the rsv nucleoprotein in complex with C-terminal peptide of the phosphoprotein
Analyse N-terminal globular domain of the rsv nucleoprotein in complex with C-terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UCB
- Type
- protein
- Length
- 440 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein; Phosphosprotein
- UniProt
- P03418, P03421
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 3 distinct chains · 63% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoprotein | protein | 219 | 61% helix, 9% strand | P03418 |
| B | Nucleoprotein | protein | 219 | 64% helix, 5% strand | P03418 |
| C, D | Phosphosprotein | protein | 1 | 0% helix, 0% strand | P03421 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.61 | 0.78 | 29 | empty |
| 2 | 401 | 0.60 | 0.76 | 36 | SO4 |
| 3 | 79 | 0.39 | 0.77 | 17 | empty |
| 4 | 72 | 0.35 | 0.76 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 443 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 188 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 187 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4UCB · N-terminal globular domain of the RSV Nucleoprotein in complex with C- terminal peptide… · 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 P03418
- Every structure of UniProt P03421
- Elsewhere: RCSB PDB 4UCB · PDBe 4UCB · UniProt P03418 · UniProt P03421
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