Research workbench
Tetramerization domain of measles virus phosphoprotein
Analyse Tetramerization domain of measles virus phosphoprotein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZDO
- Type
- protein
- Length
- 505 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoprotein
- UniProt
- Q83623
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 5 distinct chains · 96% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoprotein | protein | 63 | 95% helix, 0% strand | Q83623 |
| B, E, H | Phosphoprotein | protein | 62 | 97% helix, 0% strand | Q83623 |
| C | Phosphoprotein | protein | 63 | 97% helix, 0% strand | Q83623 |
| D, G | Phosphoprotein | protein | 64 | 94% helix, 0% strand | Q83623 |
| F | Phosphoprotein | protein | 65 | 95% helix, 0% strand | Q83623 |
Ligands and binding sites
- MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.59 | 0.81 | 20 | MRD |
| 2 | 107 | 0.45 | 0.79 | 16 | empty |
| 3 | 92 | 0.42 | 0.78 | 20 | empty |
Interfaces
20 interfaces between chains.
- E–F · 1609 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 1588 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1545 Ų buried · 12 hydrogen bonds · protein-protein
- G–H · 1528 Ų buried · 15 hydrogen bonds · protein-protein
- F–G · 1484 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3ZDO · Tetramerization domain of Measles virus phosphoprotein · 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 Q83623
- Elsewhere: RCSB PDB 3ZDO · PDBe 3ZDO · UniProt Q83623
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