Research workbench
The CAS13B binary complex
Analyse The CAS13B binary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AAY
- Type
- protein + RNA
- Length
- 1,251 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bergeyella zoohelcum CAS13B (R1177A) mutant; RNA (52-mer)
- UniProt
- K1LVU1
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bergeyella zoohelcum CAS13B (R1177A) mutant | protein | 1199 | 53% helix, 7% strand | K1LVU1 |
| B | RNA (52-mer) | rna | 52 | — | — |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 627 | 0.85 | 0.90 | 61 | empty |
| 2 | 1077 | 0.83 | 0.85 | 96 | empty |
| 3 | 486 | 0.83 | 0.90 | 55 | empty |
| 4 | 626 | 0.79 | 0.84 | 70 | empty |
| 5 | 393 | 0.76 | 0.87 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 5430 Ų buried · 94 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 6AAY · the Cas13b binary complex · 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 K1LVU1
- Elsewhere: RCSB PDB 6AAY · PDBe 6AAY · UniProt K1LVU1
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