MolNFT v1 · #113244 · protein
Cryo-electron tomography and subtomogram averaging of rous-sarcoma- virus deltambd virus-like particles
5A9E · Deltambd gag protein: “Cryo-electron tomography and subtomogram averaging of rous-sarcoma- virus deltambd virus-like particles”. Electron microscopy, 20 pockets (best druggability 0.57). MolNFT v1 #113244 on GenesisL1: 3D structure…
- PDB
- 5A9E
- Type
- protein
- Length
- 4,356 residues
- Chains
- 18
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deltambd gag protein
- UniProt
- P03322
- Pockets
- 20 · best druggability 0.57
Structure
electron microscopy · 2 distinct chains · 59% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Deltambd gag protein | protein | 255 | 56% helix, 0% strand | P03322 |
| M, N, O, P, Q, R | Deltambd gag protein | protein | 216 | 63% helix, 0% strand | P03322 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 544 | 0.57 | 0.73 | 83 | empty |
| 2 | 522 | 0.56 | 0.73 | 94 | empty |
| 3 | 504 | 0.56 | 0.73 | 65 | empty |
| 4 | 517 | 0.55 | 0.72 | 81 | empty |
| 5 | 408 | 0.53 | 0.73 | 65 | empty |
Interfaces
36 interfaces between chains.
- L–M · 229 Ų buried · 2 hydrogen bonds · protein-protein
- A–G · 184 Ų buried · 0 hydrogen bonds · protein-protein
- K–R · 174 Ų buried · 4 hydrogen bonds · protein-protein
- H–O · 173 Ų buried · 2 hydrogen bonds · protein-protein
- J–Q · 168 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5A9E · Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD… · 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 P03322
- Elsewhere: RCSB PDB 5A9E · PDBe 5A9E · UniProt P03322
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