Research workbench
Structure of the rhodobacter capsulatus CAS13A-crrna binary complex
Analyse Structure of the rhodobacter capsulatus CAS13A-crrna binary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OS0
- Type
- protein + RNA
- Length
- 2,347 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CAS13A; Crrna
- UniProt
- D5AUW0
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 62% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CAS13A | protein | 1130 | 62% helix, 5% strand | D5AUW0 |
| C | CAS13A | protein | 1123 | 62% helix, 5% strand | D5AUW0 |
| D, F | Crrna | rna | 47 | — | — |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 11 copies · chains A, F, C, D
- BME · Beta-mercaptoethanol · additive · 3 copies · chains A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 839 | 0.87 | 0.90 | 127 | EDO |
| 2 | 368 | 0.82 | 0.91 | 53 | empty |
| 3 | 574 | 0.82 | 0.88 | 72 | EDO |
| 4 | 397 | 0.81 | 0.90 | 64 | empty |
| 5 | 577 | 0.81 | 0.87 | 63 | empty |
Interfaces
3 interfaces between chains.
- A–F · 6228 Ų buried · 131 hydrogen bonds · protein-nucleic
- C–D · 6089 Ų buried · 135 hydrogen bonds · protein-nucleic
- A–C · 670 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7OS0 · Structure of the Rhodobacter capsulatus Cas13a-crRNA 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 D5AUW0
- Elsewhere: RCSB PDB 7OS0 · PDBe 7OS0 · UniProt D5AUW0
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