Research workbench
Cryo-EM structure of CRISPR-CAS surveillance complex with ACRIF14
Analyse Cryo-EM structure of CRISPR-CAS surveillance complex with ACRIF14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JZZ
- Type
- protein + RNA
- Length
- 3,038 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; Type I-F…
- UniProt
- Q02ML9, B3G161, A0A643HZS6, A0A444M080
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 8 distinct chains · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated protein CSY1 | protein | 427 | 47% helix, 5% strand | Q02ML9 |
| B | Type I-F CRISPR-associated protein CSY2 | protein | 306 | 23% helix, 30% strand | B3G161 |
| C | Type I-F CRISPR-associated endoribonuclease CAS6/CSY4 | protein | 187 | 28% helix, 26% strand | A0A643HZS6 |
| D | CRISPR type I-F/YPEST-associated protein CSY3 | protein | 298 | 25% helix, 26% strand | A0A444M080 |
| E, F, G, I | CRISPR type I-F/YPEST-associated protein CSY3 | protein | 335 | 25% helix, 27% strand | A0A444M080 |
| H | CRISPR type I-F/YPEST-associated protein CSY3 | protein | 330 | 25% helix, 26% strand | A0A444M080 |
| J, K | ACRF14 | protein | 45 | 24% helix, 33% strand | — |
| M | RNA (61-mer) | rna | 60 | — | — |
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 | 985 | 0.85 | 0.86 | 122 | empty |
| 2 | 434 | 0.82 | 0.90 | 57 | empty |
| 3 | 943 | 0.81 | 0.83 | 114 | empty |
| 4 | 608 | 0.81 | 0.86 | 77 | empty |
| 5 | 1175 | 0.80 | 0.82 | 114 | empty |
Interfaces
34 interfaces between chains.
- A–B · 4577 Ų buried · 58 hydrogen bonds · protein-protein
- B–I · 2159 Ų buried · 33 hydrogen bonds · protein-protein
- F–G · 2132 Ų buried · 34 hydrogen bonds · protein-protein
- H–I · 2055 Ų buried · 37 hydrogen bonds · protein-protein
- G–H · 2055 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 7JZZ · Cryo-EM structure of CRISPR-Cas surveillance complex with AcrIF14 · the same entry in another collection · chain M against M, 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 A0A643HZS6
- Every structure of UniProt A0A444M080
- Elsewhere: RCSB PDB 7JZZ · PDBe 7JZZ · UniProt Q02ML9 · UniProt B3G161 · UniProt A0A643HZS6 · UniProt A0A444M080
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