Research workbench
Icosahedral asymmetric unit (iasu) model of the less refined, coarse part of fhv eluted particle
Analyse Icosahedral asymmetric unit (iasu) model of the less refined, coarse part of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ITF
- Type
- protein
- Length
- 519 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
- 6 · best druggability 0.71
Structure
electron microscopy · 3 distinct chains · 8% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid protein beta (EC 3.4.23.44) | protein | 191 | 9% helix, 21% strand | P12870 |
| B | Capsid protein beta (EC 3.4.23.44) | protein | 168 | 10% helix, 14% strand | P12870 |
| C | Capsid protein beta (EC 3.4.23.44) | protein | 160 | 6% helix, 15% strand | P12870 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 730 | 0.71 | 0.78 | 81 | empty |
| 2 | 441 | 0.71 | 0.81 | 47 | empty |
| 3 | 567 | 0.69 | 0.78 | 71 | empty |
| 4 | 109 | 0.43 | 0.77 | 22 | empty |
| 5 | 136 | 0.42 | 0.74 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1047 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 811 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 611 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 6ITF · Icosahedral asymmetric unit (iASU) model of the less refined, coarse part of FHV eluted… · 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 P12870
- Elsewhere: RCSB PDB 6ITF · PDBe 6ITF · UniProt P12870
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