Research workbench
Crystal structure of CSM3-CSM4 subcomplex in the type III-a CRISPR-CAS interference complex
Analyse Crystal structure of CSM3-CSM4 subcomplex in the type III-a CRISPR-CAS… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QTS
- Type
- protein
- Length
- 979 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR type III-associated ramp protein CSM4; CRISPR type III-associated ramp protein CSM3
- UniProt
- Q59062, Q59063
- Ligands
- ZN
- Pockets
- 10 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 28% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR type III-associated ramp protein CSM4 | protein | 311 | 27% helix, 32% strand | Q59062 |
| B | CRISPR type III-associated ramp protein CSM4 | protein | 308 | 29% helix, 31% strand | Q59062 |
| C | CRISPR type III-associated ramp protein CSM3 | protein | 186 | 28% helix, 31% strand | Q59063 |
| D | CRISPR type III-associated ramp protein CSM3 | protein | 174 | 29% helix, 28% strand | Q59063 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1150 | 0.74 | 0.77 | 106 | empty |
| 2 | 362 | 0.64 | 0.79 | 47 | empty |
| 3 | 614 | 0.62 | 0.74 | 66 | empty |
| 4 | 60 | 0.56 | 0.89 | 12 | empty |
| 5 | 73 | 0.54 | 0.86 | 21 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1950 Ų buried · 21 hydrogen bonds · protein-protein
- B–D · 1042 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 1028 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 18 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 17 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4QTS · Crystal structure of Csm3-Csm4 subcomplex in the type III-A CRISPR-Cas interference… · the same entry in another collection · chain D against D, TM-score 1.00
- Q59063 · AlphaFold monomer V2.0 prediction for CRISPR system cms endoribonuclease CSM3 (Q59063) · a predicted model of the same protein · chain D against A, TM-score 0.96
- Q59062 · AlphaFold monomer V2.0 prediction for CRISPR system cms protein CSM4 (Q59062) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q59062
- Every structure of UniProt Q59063
- Elsewhere: RCSB PDB 4QTS · PDBe 4QTS · UniProt Q59062 · UniProt Q59063
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.