Research workbench
Cryoem structure of ACRIIA2 in complex with CRISPR-CAS9
Analyse Cryoem structure of ACRIIA2 in complex with CRISPR-CAS9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MCB
- Type
- protein + RNA
- Length
- 1,603 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Single guide RNA (116-mer); CRISPR-associated endonuclease CAS9; Anti-CRISPR protein…
- EC
- 3.1.-.-
- UniProt
- J7M7J1
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 3 distinct chains · 40% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Single guide RNA (116-mer) | rna | 116 | — | — |
| A | CRISPR-associated endonuclease CAS9 (EC 3.1.-.-) | protein | 1364 | 42% helix, 11% strand | J7M7J1 |
| C | Anti-CRISPR protein ACRIIA2 | protein | 123 | 20% helix, 24% strand | — |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1078 | 0.86 | 0.88 | 101 | empty |
| 2 | 596 | 0.85 | 0.90 | 79 | empty |
| 3 | 826 | 0.79 | 0.82 | 82 | empty |
| 4 | 189 | 0.72 | 0.89 | 29 | empty |
| 5 | 66 | 0.72 | 0.98 | 21 | empty |
Interfaces
3 interfaces between chains.
- B–A · 7560 Ų buried · 165 hydrogen bonds · protein-nucleic
- A–C · 1811 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 100 Ų buried · 1 hydrogen bond · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 6MCB · CryoEM structure of AcrIIA2 in complex with CRISPR-Cas9 · the same entry in another collection · chain B against B, 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 J7M7J1
- Elsewhere: RCSB PDB 6MCB · PDBe 6MCB · UniProt J7M7J1
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