Research workbench
Anti-CRISPR associated (aca) protein, ACA2
Analyse Anti-CRISPR associated (aca) protein, ACA2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B5J
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-CRISPR associated (aca) protein, ACA2
- UniProt
- H9C180
- Pockets
- 3 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Anti-CRISPR associated (aca) protein, ACA2 | protein | 115 | 67% helix, 3% strand | H9C180 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.45 | 0.78 | 23 | empty |
| 2 | 107 | 0.38 | 0.75 | 18 | empty |
| 3 | 95 | 0.36 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1264 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 7B5J · Anti-CRISPR associated (Aca) protein, Aca2 · 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 H9C180
- Elsewhere: RCSB PDB 7B5J · PDBe 7B5J · UniProt H9C180
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