MolNFT v1 · #86811 · protein
Measles virus phosphoprotein tetramerization domain
4BHV: “Measles virus phosphoprotein tetramerization domain”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.54). MolNFT v1 #86811 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4BHV
- Type
- protein
- Length
- 228 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoprotein
- UniProt
- P35974
- Ligands
- CA
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 3 distinct chains · 92% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Phosphoprotein | protein | 57 | 93% helix, 0% strand | P35974 |
| B | Phosphoprotein | protein | 56 | 91% helix, 0% strand | P35974 |
| D | Phosphoprotein | protein | 58 | 93% helix, 0% strand | P35974 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A, B, C, D
- ACT · Acetate ion · additive · 4 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.54 | 0.81 | 21 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1297 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 1270 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 1248 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 1187 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 85 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4BHV · Measles virus 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 P35974
- Elsewhere: RCSB PDB 4BHV · PDBe 4BHV · UniProt P35974
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