Research workbench
Structure of csy-ACRIF24-dsdna
Analyse Structure of csy-ACRIF24-dsdna in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ELN
- Type
- protein + DNA + RNA
- Length
- 6,381 residues
- Chains
- 26
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR type I-F/YPEST-associated protein CSY2; CRISPR-associated protein CSY3; Type I-F…
- UniProt
- B3G161, A0A659BSG0, A0A3A8DDU9
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 15 distinct chains · 28% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, L | CRISPR type I-F/YPEST-associated protein CSY2 | protein | 305 | 23% helix, 30% strand | B3G161 |
| C, M | CRISPR-associated protein CSY3 | protein | 293 | 26% helix, 26% strand | A0A659BSG0 |
| D, O | CRISPR-associated protein CSY3 | protein | 334 | 25% helix, 23% strand | A0A659BSG0 |
| E | CRISPR-associated protein CSY3 | protein | 337 | 24% helix, 26% strand | A0A659BSG0 |
| F, P | CRISPR-associated protein CSY3 | protein | 335 | 25% helix, 26% strand | A0A659BSG0 |
| G | CRISPR-associated protein CSY3 | protein | 329 | 26% helix, 25% strand | A0A659BSG0 |
| H | CRISPR-associated protein CSY3 | protein | 332 | 25% helix, 25% strand | A0A659BSG0 |
| I, S | Type I-F CRISPR-associated endoribonuclease CAS6/CSY4 | protein | 187 | 25% helix, 25% strand | — |
| N | CRISPR-associated protein CSY3 | protein | 335 | 25% helix, 24% strand | A0A659BSG0 |
| Q, R | CRISPR-associated protein CSY3 | protein | 333 | 26% helix, 25% strand | A0A659BSG0 |
| U, V | ACRIF24 | protein | 227 | 29% helix, 22% strand | — |
| J, T | RNA (60-mer) | rna | 60 | — | — |
| A, X | Type I-F CRISPR-associated protein CSY1 | protein | 424 | 51% helix, 7% strand | A0A3A8DDU9 |
| K, Y | 54-mer DNA | dna | 13 | — | — |
| W, Z | 54-mer DNA | dna | 13 | — | — |
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 | 903 | 0.86 | 0.88 | 117 | empty |
| 2 | 1169 | 0.85 | 0.87 | 129 | empty |
| 3 | 703 | 0.85 | 0.89 | 63 | empty |
| 4 | 625 | 0.84 | 0.89 | 65 | empty |
| 5 | 344 | 0.84 | 0.93 | 50 | empty |
Interfaces
78 interfaces between chains.
- L–X · 3692 Ų buried · 33 hydrogen bonds · protein-protein
- B–A · 3534 Ų buried · 30 hydrogen bonds · protein-protein
- E–F · 2248 Ų buried · 31 hydrogen bonds · protein-protein
- N–O · 2221 Ų buried · 32 hydrogen bonds · protein-protein
- F–G · 2096 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
- 7ELN · Structure of Csy-AcrIF24-dsDNA · the same entry in another collection · chain C against C, 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 B3G161
- Every structure of UniProt A0A659BSG0
- Every structure of UniProt A0A3A8DDU9
- Elsewhere: RCSB PDB 7ELN · PDBe 7ELN · UniProt B3G161 · UniProt A0A659BSG0 · UniProt A0A3A8DDU9
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