Research workbench
Capsid protein and C-terminal part of scaffolding protein in the staphylococcus aureus phage 80ALPHA procapsid
Analyse Capsid protein and C-terminal part of scaffolding protein in the staphylococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B0X
- Type
- protein
- Length
- 2,097 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major head protein; Scaffold protein
- UniProt
- A4ZFB3, A4ZFB2
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 4 distinct chains · 30% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Major head protein | protein | 284 | 26% helix, 14% strand | A4ZFB3 |
| a | Scaffold protein | protein | 14 | 50% helix, 0% strand | A4ZFB2 |
| b, d, e, f, g | Scaffold protein | protein | 16 | 56% helix, 0% strand | A4ZFB2 |
| c | Scaffold protein | protein | 15 | 53% helix, 0% strand | A4ZFB2 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 882 | 0.85 | 0.87 | 81 | empty |
| 2 | 1105 | 0.83 | 0.84 | 97 | empty |
| 3 | 1083 | 0.77 | 0.80 | 121 | empty |
| 4 | 72 | 0.73 | 0.97 | 23 | empty |
| 5 | 737 | 0.65 | 0.74 | 56 | empty |
Interfaces
21 interfaces between chains.
- F–G · 1775 Ų buried · 18 hydrogen bonds · protein-protein
- B–G · 1768 Ų buried · 22 hydrogen bonds · protein-protein
- D–E · 1765 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 1601 Ų buried · 18 hydrogen bonds · protein-protein
- E–F · 1540 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6B0X · Capsid protein and C-terminal part of scaffolding protein in the Staphylococcus aureus… · 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 A4ZFB3
- Every structure of UniProt A4ZFB2
- Elsewhere: RCSB PDB 6B0X · PDBe 6B0X · UniProt A4ZFB3 · UniProt A4ZFB2
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