Research workbench
Cryo-EM structure of anti-CRISPR ACRIF9, bound to the type I-F crrna- guided CRISPR surveillance complex
Analyse Cryo-EM structure of anti-CRISPR ACRIF9, bound to the type I-F crrna- guided… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W1X
- Type
- protein + RNA
- Length
- 2,934 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated protein CSY1; Type I-F CRISPR-associated protein CSY2…
- EC
- 3.1.-.-
- UniProt
- Q02ML9, B3G161, A0A444M080, Q02MM2, C0AVY5
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 11 distinct chains · 29% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated protein CSY1 | protein | 314 | 43% helix, 7% strand | Q02ML9 |
| B | Type I-F CRISPR-associated protein CSY2 | protein | 304 | 25% helix, 28% strand | B3G161 |
| C | CRISPR-associated protein CSY3 | protein | 290 | 29% helix, 23% strand | A0A444M080 |
| D | CRISPR-associated protein CSY3 | protein | 328 | 28% helix, 24% strand | A0A444M080 |
| E | CRISPR-associated protein CSY3 | protein | 329 | 28% helix, 22% strand | A0A444M080 |
| F | CRISPR-associated protein CSY3 | protein | 335 | 27% helix, 23% strand | A0A444M080 |
| G | CRISPR-associated protein CSY3 | protein | 326 | 28% helix, 25% strand | A0A444M080 |
| H | CRISPR-associated protein CSY3 | protein | 333 | 28% helix, 21% strand | A0A444M080 |
| M | RNA (60-mer) | rna | 60 | — | — |
| L | CRISPR-associated endonuclease CAS6/CSY4 (EC 3.1.-.-) | protein | 187 | 27% helix, 21% strand | Q02MM2 |
| I, J | Anti-CRISPR ACRIF9 | protein | 64 | 16% helix, 38% strand | C0AVY5 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 803 | 0.85 | 0.87 | 96 | empty |
| 2 | 789 | 0.85 | 0.88 | 104 | empty |
| 3 | 799 | 0.84 | 0.87 | 101 | empty |
| 4 | 1188 | 0.83 | 0.84 | 99 | empty |
| 5 | 1066 | 0.79 | 0.81 | 93 | empty |
Interfaces
31 interfaces between chains.
- A–B · 3569 Ų buried · 32 hydrogen bonds · protein-protein
- F–G · 2016 Ų buried · 27 hydrogen bonds · protein-protein
- E–F · 2013 Ų buried · 30 hydrogen bonds · protein-protein
- D–E · 1979 Ų buried · 25 hydrogen bonds · protein-protein
- G–H · 1943 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 6W1X · Cryo-EM structure of anti-CRISPR AcrIF9, bound to the type I-F crRNA-guided CRISPR… · the same entry in another collection · chain J against J, 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 Q02ML9
- Every structure of UniProt B3G161
- Every structure of UniProt A0A444M080
- Every structure of UniProt Q02MM2
- Every structure of UniProt C0AVY5
- Elsewhere: RCSB PDB 6W1X · PDBe 6W1X · UniProt Q02ML9 · UniProt B3G161 · UniProt A0A444M080 · UniProt Q02MM2 · UniProt C0AVY5
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