Research workbench
CAS6 (TTHB231) product complex
Analyse CAS6 (TTHB231) product complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C9D
- Type
- protein + RNA
- Length
- 547 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CAS6B; R3 repeat RNA cleavage product
- UniProt
- Q53VU8
- Pockets
- 11 · best druggability 0.70
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CAS6B | protein | 262 | 34% helix, 30% strand | Q53VU8 |
| B | CAS6B | protein | 260 | 36% helix, 32% strand | Q53VU8 |
| C | R3 repeat RNA cleavage product | rna | 12 | — | — |
| D | R3 repeat RNA cleavage product | rna | 13 | — | — |
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 355 | 0.70 | 0.83 | 43 | empty |
| 2 | 113 | 0.64 | 0.89 | 28 | empty |
| 3 | 93 | 0.58 | 0.87 | 22 | empty |
| 4 | 78 | 0.48 | 0.83 | 21 | empty |
| 5 | 193 | 0.48 | 0.75 | 31 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1072 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 971 Ų buried · 23 hydrogen bonds · protein-nucleic
- A–C · 960 Ų buried · 27 hydrogen bonds · protein-nucleic
- B–C · 105 Ų buried · 4 hydrogen bonds · protein-nucleic
- A–D · 102 Ų buried · 3 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 2 modified (nucleotide modification).
Compared structures
- 4C9D · Cas6 (TTHB231) product 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 Q53VU8
- Elsewhere: RCSB PDB 4C9D · PDBe 4C9D · UniProt Q53VU8
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