Research workbench
Cryo-EM structure of CRISPR-CAS surveillance complex with ACRIF7
Analyse Cryo-EM structure of CRISPR-CAS surveillance complex with ACRIF7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JZX
- Type
- protein + RNA
- Length
- 3,014 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated endonuclease CAS6/CSY4; Type I-F CRISPR-associated protein CSY2; CRISPR…
- EC
- 3.1.-.-
- UniProt
- Q02MM2, B3G161, A0A444M080, Q02ML9, B3G1L5
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 8 distinct chains · 29% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | CRISPR-associated endonuclease CAS6/CSY4 (EC 3.1.-.-) | protein | 187 | 27% helix, 25% strand | Q02MM2 |
| B | Type I-F CRISPR-associated protein CSY2 | protein | 306 | 22% helix, 30% strand | B3G161 |
| E, F, G, I | CRISPR type I-F/YPEST-associated protein CSY3 | protein | 335 | 25% helix, 24% strand | A0A444M080 |
| D | CRISPR type I-F/YPEST-associated protein CSY3 | protein | 298 | 23% helix, 26% strand | A0A444M080 |
| H | CRISPR type I-F/YPEST-associated protein CSY3 | protein | 330 | 24% helix, 25% strand | A0A444M080 |
| A | CRISPR-associated protein CSY1 | protein | 427 | 47% helix, 6% strand | Q02ML9 |
| M | RNA (61-mer) | rna | 60 | — | — |
| J | ACRF7 | protein | 66 | 26% helix, 23% strand | B3G1L5 |
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 | 391 | 0.82 | 0.91 | 49 | empty |
| 2 | 774 | 0.79 | 0.83 | 96 | empty |
| 3 | 894 | 0.79 | 0.82 | 102 | empty |
| 4 | 845 | 0.78 | 0.82 | 78 | empty |
| 5 | 504 | 0.78 | 0.85 | 55 | empty |
Interfaces
25 interfaces between chains.
- B–A · 4708 Ų buried · 56 hydrogen bonds · protein-protein
- G–H · 2181 Ų buried · 30 hydrogen bonds · protein-protein
- F–G · 2134 Ų buried · 37 hydrogen bonds · protein-protein
- E–D · 2106 Ų buried · 32 hydrogen bonds · protein-protein
- H–I · 2087 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 7JZX · Cryo-EM structure of CRISPR-Cas surveillance complex with AcrIF7 · the same entry in another collection · chain J against J, TM-score 1.00
- Q02MM2 · AlphaFold monomer V2.0 prediction for CRISPR-associated endonuclease CAS6/CSY4 (Q02MM2) · a predicted model of the same protein · chain C against A, TM-score 0.98
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 Q02MM2
- Every structure of UniProt B3G161
- Every structure of UniProt A0A444M080
- Every structure of UniProt Q02ML9
- Every structure of UniProt B3G1L5
- Elsewhere: RCSB PDB 7JZX · PDBe 7JZX · UniProt Q02MM2 · UniProt B3G161 · UniProt A0A444M080 · UniProt Q02ML9 · UniProt B3G1L5
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