MolNFT v1 · #152782 · protein
Icosahedral asymmetric unit (iasu) model of the well-refined part of fhv eluted particle
6ITB · Capsid protein beta: “Icosahedral asymmetric unit (iasu) model of the well-refined part of fhv eluted particle”. Electron microscopy, 10 pockets (best druggability 0.84). MolNFT v1 #152782 on GenesisL1: 3D structure, binding sites…
- PDB
- 6ITB
- Type
- protein
- Length
- 821 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein beta
- EC
- 3.4.23.44
- UniProt
- P12870
- Pockets
- 10 · best druggability 0.84
Structure
electron microscopy · 3 distinct chains · 10% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid protein beta (EC 3.4.23.44) | protein | 263 | 7% helix, 42% strand | P12870 |
| B | Capsid protein beta (EC 3.4.23.44) | protein | 266 | 9% helix, 46% strand | P12870 |
| C | Capsid protein beta (EC 3.4.23.44) | protein | 292 | 14% helix, 37% strand | P12870 |
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1117 | 0.84 | 0.86 | 75 | empty |
| 2 | 95 | 0.78 | 0.98 | 25 | empty |
| 3 | 79 | 0.76 | 0.98 | 27 | empty |
| 4 | 330 | 0.74 | 0.85 | 35 | empty |
| 5 | 250 | 0.67 | 0.83 | 23 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1578 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 1547 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1362 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6ITB · Icosahedral asymmetric unit (iASU) model of the well-refined part of FHV eluted particle · the same entry in another collection · chain B against B, 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 P12870
- Elsewhere: RCSB PDB 6ITB · PDBe 6ITB · UniProt P12870
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