Research workbench
Crystal structure of anti-CRISPR protein ACRF1
Analyse Crystal structure of anti-CRISPR protein ACRF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ANV
- Type
- protein
- Length
- 902 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-CRISPR protein ACRF1 fused with C-terminal mbp tag
- UniProt
- L7P7M1, P0AEY0
- Ligands
- GLC
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Anti-CRISPR protein ACRF1 fused with C-terminal mbp tag | protein | 451 | 43% helix, 23% strand | L7P7M1, P0AEY0 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains A, B
- PGE · Triethylene glycol · additive · 3 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.79 | 0.81 | 75 | GLC, MES, PGE, EDO |
| 2 | 817 | 0.79 | 0.82 | 54 | GLC, MES, PEG |
| 3 | 200 | 0.54 | 0.78 | 37 | EDO |
| 4 | 250 | 0.50 | 0.74 | 31 | PGE, PEG |
| 5 | 228 | 0.50 | 0.75 | 25 | PGE |
Interfaces
1 interface between chains.
- A–B · 20 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6ANV · Crystal structure of anti-CRISPR protein AcrF1 · 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 L7P7M1
- Every structure of UniProt P0AEY0
- Elsewhere: RCSB PDB 6ANV · PDBe 6ANV · UniProt L7P7M1 · UniProt P0AEY0
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