MolNFT v1 · #127378 · protein
Dsrna bacteriophage PHI6 nucleocapsid
5MUU · Major inner protein P1: “Dsrna bacteriophage PHI6 nucleocapsid”. Electron microscopy, 20 pockets (best druggability 0.87). MolNFT v1 #127378 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5MUU
- Type
- protein
- Length
- 3,051 residues
- Chains
- 13
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major inner protein P1; Packaging enzyme P4; Major outer capsid protein
- EC
- 3.6.1.15
- UniProt
- P11126, P11125, P07579
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 3 distinct chains · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Major inner protein P1 | protein | 766 | 49% helix, 12% strand | P11126 |
| C | Packaging enzyme P4 (EC 3.6.1.15) | protein | 39 | 18% helix, 5% strand | P11125 |
| D, E, F, G, H, I, J, K, L, M | Major outer capsid protein | protein | 148 | 75% helix, 0% strand | P07579 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 651 | 0.87 | 0.91 | 84 | empty |
| 2 | 756 | 0.81 | 0.84 | 71 | empty |
| 3 | 419 | 0.75 | 0.84 | 55 | empty |
| 4 | 109 | 0.74 | 0.94 | 25 | empty |
| 5 | 63 | 0.72 | 0.97 | 24 | empty |
Interfaces
34 interfaces between chains.
- B–C · 1760 Ų buried · 11 hydrogen bonds · protein-protein
- K–M · 1436 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1385 Ų buried · 11 hydrogen bonds · protein-protein
- J–L · 1038 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 1018 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5MUU · dsRNA bacteriophage phi6 nucleocapsid · 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 P11126
- Every structure of UniProt P11125
- Every structure of UniProt P07579
- Elsewhere: RCSB PDB 5MUU · PDBe 5MUU · UniProt P11126 · UniProt P11125 · UniProt P07579
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