Research workbench
V. cholerae tniq-cascade complex, open conformation
Analyse V. cholerae tniq-cascade complex, open conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PIF
- Type
- protein + RNA
- Length
- 3,508 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CAS7, type I-F CRISPR-associated protein; CAS5_8 naturally occurring fusion protein; Type…
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 9 distinct chains · 21% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CAS7, type I-F CRISPR-associated protein | protein | 343 | 23% helix, 21% strand | — |
| B | CAS7, type I-F CRISPR-associated protein | protein | 339 | 16% helix, 23% strand | — |
| C, D, E | CAS7, type I-F CRISPR-associated protein | protein | 338 | 19% helix, 21% strand | — |
| F | CAS7, type I-F CRISPR-associated protein | protein | 310 | 19% helix, 22% strand | — |
| G | CAS5_8 naturally occurring fusion protein | protein | 521 | 15% helix, 15% strand | — |
| H | Type I-F CRISPR-associated endoribonuclease CAS6/CSY4 | protein | 198 | 18% helix, 12% strand | — |
| I | Tniq monomer 1 | protein | 355 | 30% helix, 2% strand | — |
| J | Tniq monomer 2 | protein | 368 | 30% helix, 3% strand | — |
| 1 | Guide RNA (60-mer) | rna | 60 | — | — |
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 | 876 | 0.85 | 0.87 | 85 | empty |
| 2 | 1096 | 0.79 | 0.81 | 104 | empty |
| 3 | 998 | 0.77 | 0.79 | 76 | empty |
| 4 | 95 | 0.76 | 0.97 | 21 | empty |
| 5 | 875 | 0.75 | 0.79 | 80 | empty |
Interfaces
26 interfaces between chains.
- C–D · 2352 Ų buried · 21 hydrogen bonds · protein-protein
- D–E · 2305 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 2248 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 2217 Ų buried · 20 hydrogen bonds · protein-protein
- E–F · 2208 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 isopeptide (isopeptide).
Compared structures
- 6PIF · V. cholerae TniQ-Cascade complex, open conformation · 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
- Elsewhere: RCSB PDB 6PIF · PDBe 6PIF
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