Research workbench
Structure of the lactococcus lactis csm CTR_3:2 CRISPR-CAS complex
Analyse Structure of the lactococcus lactis csm CTR_3:2 CRISPR-CAS complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XN4
- Type
- protein + RNA
- Length
- 2,299 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated protein CSM4; CRISPR-associated protein CSM3; CRISPR RNA…
- UniProt
- L0CFH1, L0CEA3, L0CFW2, L0CEJ3, L0CG31
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 9 distinct chains · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | CRISPR-associated protein CSM4 | protein | 275 | 14% helix, 29% strand | L0CFH1 |
| F | CRISPR-associated protein CSM3 | protein | 207 | 21% helix, 28% strand | L0CEA3 |
| H, G | CRISPR-associated protein CSM3 | protein | 214 | 24% helix, 28% strand | L0CEA3 |
| R | CRISPR RNA | rna | 35 | — | — |
| C | CRISPR-associated protein CSM2 | protein | 139 | 64% helix, 6% strand | L0CFW2 |
| D | CRISPR-associated protein CSM2 | protein | 135 | 67% helix, 4% strand | L0CFW2 |
| T | Target RNA | rna | 30 | — | — |
| A | CRISPR-associated protein CAS10 | protein | 741 | 44% helix, 10% strand | L0CEJ3 |
| J | CRISPR-associated protein CSM5 | protein | 309 | 24% helix, 21% strand | L0CG31 |
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 | 725 | 0.89 | 0.93 | 100 | empty |
| 2 | 882 | 0.85 | 0.87 | 84 | empty |
| 3 | 450 | 0.83 | 0.90 | 53 | empty |
| 4 | 293 | 0.82 | 0.93 | 47 | empty |
| 5 | 128 | 0.79 | 0.96 | 29 | empty |
Interfaces
33 interfaces between chains.
- B–R · 1544 Ų buried · 40 hydrogen bonds · protein-nucleic
- F–G · 1416 Ų buried · 18 hydrogen bonds · protein-protein
- B–F · 1307 Ų buried · 13 hydrogen bonds · protein-protein
- H–G · 1303 Ų buried · 13 hydrogen bonds · protein-protein
- B–A · 1301 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6XN4 · Structure of the Lactococcus lactis Csm CTR_3:2 CRISPR-Cas Complex · the same entry in another collection · chain B against B, 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 L0CFH1
- Every structure of UniProt L0CEA3
- Every structure of UniProt L0CFW2
- Every structure of UniProt L0CEJ3
- Every structure of UniProt L0CG31
- Elsewhere: RCSB PDB 6XN4 · PDBe 6XN4 · UniProt L0CFH1 · UniProt L0CEA3 · UniProt L0CFW2 · UniProt L0CEJ3 · UniProt L0CG31
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