Research workbench
Structure of the lactococcus lactis csm ntr CRISPR-CAS complex
Analyse Structure of the lactococcus lactis csm ntr 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
- 6XN7
- Type
- protein + RNA
- Length
- 2,654 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated protein CAS10; CRISPR-associated protein CSM4; CRISPR-associated…
- UniProt
- L0CEJ3, L0CFH1, L0CEA3, L0CG31, L0CFW2
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 10 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated protein CAS10 | protein | 746 | 49% helix, 10% strand | L0CEJ3 |
| B | CRISPR-associated protein CSM4 | protein | 277 | 15% helix, 31% strand | L0CFH1 |
| F | CRISPR-associated protein CSM3 | protein | 207 | 24% helix, 28% strand | L0CEA3 |
| H, G, I | CRISPR-associated protein CSM3 | protein | 214 | 27% helix, 28% strand | L0CEA3 |
| J | CRISPR-associated protein CSM5 | protein | 309 | 23% helix, 20% strand | L0CG31 |
| R | CRISPR RNA | rna | 37 | — | — |
| C | CRISPR-associated protein CSM2 | protein | 139 | 63% helix, 7% strand | L0CFW2 |
| D | CRISPR-associated protein CSM2 | protein | 135 | 65% helix, 6% strand | L0CFW2 |
| E | CRISPR-associated protein CSM2 | protein | 125 | 72% helix, 2% strand | L0CFW2 |
| T | Target RNA | rna | 37 | — | — |
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 | 1173 | 0.89 | 0.90 | 120 | empty |
| 2 | 1152 | 0.87 | 0.89 | 110 | empty |
| 3 | 1187 | 0.87 | 0.88 | 103 | empty |
| 4 | 508 | 0.84 | 0.91 | 53 | empty |
| 5 | 899 | 0.83 | 0.84 | 106 | empty |
Interfaces
44 interfaces between chains.
- B–R · 1553 Ų buried · 33 hydrogen bonds · protein-nucleic
- R–T · 1413 Ų buried · 115 hydrogen bonds · nucleic-nucleic
- H–G · 1352 Ų buried · 21 hydrogen bonds · protein-protein
- F–G · 1349 Ų buried · 18 hydrogen bonds · protein-protein
- H–I · 1331 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6XN7 · Structure of the Lactococcus lactis Csm NTR CRISPR-Cas 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 L0CEJ3
- Every structure of UniProt L0CFH1
- Every structure of UniProt L0CEA3
- Every structure of UniProt L0CG31
- Every structure of UniProt L0CFW2
- Elsewhere: RCSB PDB 6XN7 · PDBe 6XN7 · UniProt L0CEJ3 · UniProt L0CFH1 · UniProt L0CEA3 · UniProt L0CG31 · UniProt L0CFW2
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