Research workbench
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 v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tail sheath protein GP18
- UniProt
- P13332
- Pockets
- 4 · best druggability 0.44
Structure
x-ray diffraction · 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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