Research workbench
Structure of human respiratory syncytial virus nonstructural protein 2 (NS2)
Analyse Structure of human respiratory syncytial virus nonstructural protein 2 (NS2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LDK
- Type
- protein
- Length
- 314 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-structural protein 2
- UniProt
- Q86305
- Ligands
- CL
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 3 distinct chains · 60% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Non-structural protein 2 | protein | 106 | 59% helix, 16% strand | Q86305 |
| A | Non-structural protein 2 | protein | 103 | 61% helix, 17% strand | Q86305 |
| C | Non-structural protein 2 | protein | 105 | 60% helix, 16% strand | Q86305 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains B, A
- TAR · D(-)-tartaric acid · additive · 3 copies · chains B, C, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.53 | 0.77 | 25 | empty |
| 2 | 239 | 0.53 | 0.76 | 39 | TAR |
| 3 | 124 | 0.46 | 0.78 | 23 | TAR |
Interfaces
3 interfaces between chains.
- B–A · 601 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 591 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 104 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 7LDK · Structure of human respiratory syncytial virus nonstructural protein 2 (NS2) · the same entry in another collection · chain B against B, 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 Q86305
- Elsewhere: RCSB PDB 7LDK · PDBe 7LDK · UniProt Q86305
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.