Research workbench
Cryo-EM structure of type III-a csm-ntr complex
Analyse Cryo-EM structure of type III-a csm-ntr complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IFL
- Type
- protein + RNA
- Length
- 2,263 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type III-a CRISPR-associated protein CSM1; Type III-a CRISPR-associated protein CSM2…
- UniProt
- A0A2U2M0F3, A0A2U2M049, A0A2U2M035, A0A2U2M037, A0A2U2M038
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 9 distinct chains · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type III-a CRISPR-associated protein CSM1 | protein | 691 | 49% helix, 11% strand | A0A2U2M0F3 |
| B, C | Type III-a CRISPR-associated protein CSM2 | protein | 121 | 67% helix, 2% strand | A0A2U2M049 |
| D | Type III-a CRISPR-associated ramp protein CSM3 | protein | 217 | 21% helix, 25% strand | A0A2U2M035 |
| E | Type III-a CRISPR-associated ramp protein CSM3 | protein | 217 | 24% helix, 30% strand | A0A2U2M035 |
| F | Type III-a CRISPR-associated ramp protein CSM3 | protein | 205 | 20% helix, 27% strand | A0A2U2M035 |
| G | Type III-a CRISPR-associated ramp protein CSM4 | protein | 273 | 19% helix, 25% strand | A0A2U2M037 |
| H | Type III-a CRISPR-associated ramp protein CSM5 | protein | 348 | 21% helix, 19% strand | A0A2U2M038 |
| I | Crrna | rna | 35 | — | — |
| J | Ntr | rna | 35 | — | — |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1160 | 0.86 | 0.87 | 101 | empty |
| 2 | 1138 | 0.83 | 0.85 | 81 | empty |
| 3 | 1120 | 0.83 | 0.85 | 98 | empty |
| 4 | 189 | 0.80 | 0.95 | 33 | empty |
| 5 | 1117 | 0.79 | 0.81 | 90 | empty |
Interfaces
35 interfaces between chains.
- G–I · 1530 Ų buried · 39 hydrogen bonds · protein-nucleic
- D–H · 1525 Ų buried · 21 hydrogen bonds · protein-protein
- F–G · 1484 Ų buried · 16 hydrogen bonds · protein-protein
- D–E · 1399 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 1345 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6IFL · Cryo-EM structure of type III-A Csm-NTR 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 A0A2U2M0F3
- Every structure of UniProt A0A2U2M049
- Every structure of UniProt A0A2U2M035
- Every structure of UniProt A0A2U2M037
- Every structure of UniProt A0A2U2M038
- Elsewhere: RCSB PDB 6IFL · PDBe 6IFL · UniProt A0A2U2M0F3 · UniProt A0A2U2M049 · UniProt A0A2U2M035 · UniProt A0A2U2M037 · UniProt A0A2U2M038
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