Research workbench
Crystal structure of the human metapneumovirus phosphoprotein tetramerization domain
Analyse Crystal structure of the human metapneumovirus phosphoprotein tetramerization… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BXT
- Type
- protein
- Length
- 199 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoprotein P
- UniProt
- Q91KZ5
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 6 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoprotein P | protein | 24 | 83% helix, 0% strand | Q91KZ5 |
| B, E, F | Phosphoprotein P | protein | 25 | 84% helix, 0% strand | Q91KZ5 |
| C | Phosphoprotein P | protein | 25 | 84% helix, 0% strand | Q91KZ5 |
| D | Phosphoprotein P | protein | 26 | 77% helix, 0% strand | Q91KZ5 |
| G | Phosphoprotein P | protein | 26 | 73% helix, 0% strand | Q91KZ5 |
| H | Phosphoprotein P | protein | 23 | 87% helix, 0% strand | Q91KZ5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.45 | 0.84 | 13 | empty |
| 2 | 131 | 0.42 | 0.75 | 19 | empty |
Interfaces
16 interfaces between chains.
- A–B · 660 Ų buried · 3 hydrogen bonds · protein-protein
- E–H · 642 Ų buried · 2 hydrogen bonds · protein-protein
- F–G · 632 Ų buried · 2 hydrogen bonds · protein-protein
- E–F · 616 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 599 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4BXT · Crystal structure of the human metapneumovirus phosphoprotein tetramerization domain · 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 Q91KZ5
- Elsewhere: RCSB PDB 4BXT · PDBe 4BXT · UniProt Q91KZ5
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