Research workbench
Structure of Gp54 from Escherichia phage Bas11
Analyse Structure of Gp54 from Escherichia phage Bas11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 9AXB
- Type
- protein
- Length
- 386 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Escherichia phage JohannLBurckhardt
- Molecule
- Gp54
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, E, F | Gp54 | protein | 64 | 0% helix, 50% strand | — |
| B | Gp54 | protein | 66 | 0% helix, 48% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.72 | 0.97 | 18 | empty |
| 2 | 265 | 0.66 | 0.82 | 31 | empty |
| 3 | 172 | 0.49 | 0.77 | 23 | empty |
Interfaces
9 interfaces between chains.
- B–C · 540 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 502 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 499 Ų buried · 8 hydrogen bonds · protein-protein
- B–F · 443 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 378 Ų buried · 6 hydrogen bonds · protein-protein
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 9AXB · PDBe 9AXB
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