Research workbench
The atomic structure of the degraded procapsid particle of the bacteriophage G4: induced structural changes in the presence of calcium ions and functional implications
Analyse The atomic structure of the degraded procapsid particle of the bacteriophage… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GFF
- Type
- protein
- Length
- 606 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacteriophage G4 capsid proteins gpf, gpg, gpj
- UniProt
- P03642, P03644, P03652
- Pockets
- 4 · best druggability 0.51
Structure
x-ray diffraction · 3 distinct chains · 15% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Bacteriophage G4 capsid proteins gpf, gpg, gpj | protein | 417 | 22% helix, 27% strand | P03642 |
| 2 | Bacteriophage G4 capsid proteins gpf, gpg, gpj | protein | 177 | 0% helix, 47% strand | P03644 |
| 3 | Bacteriophage G4 capsid proteins gpf, gpg, gpj | protein | 12 | 0% helix, 0% strand | P03652 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.51 | 0.78 | 24 | empty |
| 2 | 137 | 0.40 | 0.74 | 22 | empty |
| 3 | 84 | 0.35 | 0.75 | 18 | empty |
| 4 | 54 | 0.32 | 0.77 | 15 | empty |
Interfaces
2 interfaces between chains.
- 1–3 · 845 Ų buried · 5 hydrogen bonds · protein-protein
- 1–2 · 215 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1GFF · The atomic structure of the degraded procapsid particle of the bacteriophage G4: induced… · the same entry in another collection · chain 1 against 1, 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 P03642
- Every structure of UniProt P03644
- Every structure of UniProt P03652
- Elsewhere: RCSB PDB 1GFF · PDBe 1GFF · UniProt P03642 · UniProt P03644 · UniProt P03652
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