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Crystal structure of the bacteriophage T4 tail sheath protein, protease resistant fragment gp18PR
Analyse Crystal structure of the bacteriophage T4 tail sheath protein, protease… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FO8
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Enterobacteria phage T4
- Molecule
- Tail sheath protein Gp18
- UniProt
- P13332
- Pockets
- 4 · best druggability 0.44
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain · 21% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Tail sheath protein Gp18 | protein | 274 | 21% helix, 34% strand | P13332 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.44 | 0.76 | 25 | empty |
| 2 | 131 | 0.42 | 0.76 | 28 | empty |
| 3 | 51 | 0.29 | 0.75 | 11 | empty |
| 4 | 54 | 0.25 | 0.72 | 15 | empty |
Compared structures
- 3FO8 · Crystal structure of the bacteriophage T4 tail sheath protein, protease resistant… · the same entry in another collection · chain D against D, 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 P13332
- Elsewhere: RCSB PDB 3FO8 · PDBe 3FO8 · UniProt P13332
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