MolNFT v1 · #14160 · protein
Structural studies of bacteriophage ALPHA3 assembly, cryo-electron microscopy
1M0F · Scaffolding protein D: “Structural studies of bacteriophage ALPHA3 assembly, cryo-electron microscopy”. Electron microscopy, 2 pockets (best druggability 0.35). MolNFT v1 #14160 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1M0F
- Type
- protein
- Length
- 1,179 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Scaffolding protein D; Capsid protein F; Major spike protein G; Scaffolding protein B
- UniProt
- P08767, P31281
- Pockets
- 2 · best druggability 0.35
Structure
electron microscopy · 7 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Scaffolding protein D | protein | 143 | 0% helix, 0% strand | — |
| 2 | Scaffolding protein D | protein | 135 | 0% helix, 0% strand | — |
| 3 | Scaffolding protein D | protein | 140 | 0% helix, 0% strand | — |
| 4 | Scaffolding protein D | protein | 146 | 0% helix, 0% strand | — |
| F | Capsid protein F | protein | 360 | 0% helix, 0% strand | P08767 |
| G | Major spike protein G | protein | 187 | 0% helix, 0% strand | P31281 |
| B | Scaffolding protein B | protein | 68 | 0% helix, 0% strand | — |
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 | 97 | 0.35 | 0.72 | 30 | empty |
| 2 | 56 | 0.29 | 0.72 | 18 | empty |
Interfaces
6 interfaces between chains.
- F–B · 187 Ų buried · 0 hydrogen bonds · protein-protein
- 3–4 · 133 Ų buried · 0 hydrogen bonds · protein-protein
- 1–2 · 133 Ų buried · 0 hydrogen bonds · protein-protein
- 2–3 · 83 Ų buried · 0 hydrogen bonds · protein-protein
- 1–F · 50 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1M0F · Structural Studies of Bacteriophage alpha3 Assembly, Cryo-electron microscopy · the same entry in another collection · chain 1 against 1, 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 P08767
- Every structure of UniProt P31281
- Elsewhere: RCSB PDB 1M0F · PDBe 1M0F · UniProt P08767 · UniProt P31281
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