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Crystal structure of the bacteriophage T4 tail sheath protein, deletion mutant GP18M
Analyse Crystal structure of the bacteriophage T4 tail sheath protein, deletion mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FOA
- Type
- protein
- Length
- 1,910 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tail sheath protein GP18
- UniProt
- P13332
- Pockets
- 14 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 24% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tail sheath protein GP18 | protein | 479 | 24% helix, 27% strand | P13332 |
| B | Tail sheath protein GP18 | protein | 478 | 24% helix, 27% strand | P13332 |
| C | Tail sheath protein GP18 | protein | 477 | 23% helix, 27% strand | P13332 |
| D | Tail sheath protein GP18 | protein | 476 | 25% helix, 28% strand | P13332 |
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1163 | 0.71 | 0.75 | 105 | empty |
| 2 | 792 | 0.70 | 0.76 | 91 | empty |
| 3 | 461 | 0.62 | 0.76 | 42 | empty |
| 4 | 179 | 0.57 | 0.81 | 36 | empty |
| 5 | 174 | 0.54 | 0.79 | 36 | empty |
Interfaces
4 interfaces between chains.
- B–C · 608 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 249 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 146 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 36 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3FOA · Crystal structure of the bacteriophage T4 tail sheath protein, deletion mutant gp18M · 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 P13332
- Elsewhere: RCSB PDB 3FOA · PDBe 3FOA · UniProt P13332
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