Research workbench
Structure of a phage anti-CRISPR protein
Analyse Structure of a phage anti-CRISPR protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ARZ
- Type
- protein
- Length
- 282 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.5
- Source
- Pseudomonas phage JBD5
- Molecule
- Uncharacterized protein
- UniProt
- L7P7L6
- Ligands
- BR
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · resolution 2.5 · 3 distinct chains · 78% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 96 | 78% helix, 4% strand | L7P7L6 |
| B | Uncharacterized protein | protein | 92 | 78% helix, 4% strand | L7P7L6 |
| C | Uncharacterized protein | protein | 94 | 77% helix, 4% strand | L7P7L6 |
Ligands and binding sites
- BR · Bromide ion · ion · 5 copies · chains A, B, C
- GOL · Glycerol · additive · 2 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.41 | 0.79 | 19 | PG4, BR |
Interfaces
2 interfaces between chains.
- A–B · 2042 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 177 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 6ARZ · Structure of a phage anti-CRISPR protein · 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 L7P7L6
- Elsewhere: RCSB PDB 6ARZ · PDBe 6ARZ · UniProt L7P7L6
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