Research workbench
Cryo-EM structure of T7 bacteriophage DNA translocation gp15 core protein intermediate assembly
Analyse Cryo-EM structure of T7 bacteriophage DNA translocation gp15 core protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YSZ
- Type
- protein
- Length
- 1,896 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.6
- Source
- Escherichia phage T7
- Molecule
- Internal virion protein gp15
- UniProt
- P03725
- Pockets
- 20 · best druggability 0.66
Structure
electron microscopy · resolution 3.6 · 1 distinct chain · 72% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Internal virion protein gp15 | protein | 316 | 72% helix, 2% strand | P03725 |
Pockets
20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.66 | 0.88 | 21 | empty |
| 2 | 133 | 0.65 | 0.88 | 21 | empty |
| 3 | 136 | 0.65 | 0.88 | 22 | empty |
| 4 | 129 | 0.65 | 0.88 | 22 | empty |
| 5 | 126 | 0.63 | 0.87 | 21 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2576 Ų buried · 38 hydrogen bonds · protein-protein
- A–B · 2574 Ų buried · 38 hydrogen bonds · protein-protein
- E–F · 2570 Ų buried · 39 hydrogen bonds · protein-protein
- B–C · 2568 Ų buried · 39 hydrogen bonds · protein-protein
- A–F · 2567 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 6YSZ · Cryo-EM structure of T7 bacteriophage DNA translocation GP15 core protein intermediate… · 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 P03725
- Elsewhere: RCSB PDB 6YSZ · PDBe 6YSZ · UniProt P03725
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