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The structure of the CRISPR-associated protein, CSA3, from sulfolobus solfataricus at 1.8 ångström resolution.
Analyse The structure of the CRISPR-associated protein, CSA3, from sulfolobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WTE
- Type
- protein
- Length
- 422 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CSA3
- UniProt
- Q97Y88
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CSA3 | protein | 212 | 48% helix, 19% strand | Q97Y88 |
| B | CSA3 | protein | 210 | 50% helix, 18% strand | Q97Y88 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.72 | 0.98 | 11 | empty |
| 2 | 200 | 0.51 | 0.77 | 25 | empty |
| 3 | 126 | 0.42 | 0.76 | 28 | empty |
| 4 | 91 | 0.36 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2256 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 2WTE · The structure of the CRISPR-associated protein, Csa3, from Sulfolobus solfataricus at 1.8… · the same entry in another collection · chain A against A, TM-score 1.00
- Q97Y88 · AlphaFold monomer V2.0 prediction for CRISPR locus-related putative DNA-binding protein… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q97Y88
- Elsewhere: RCSB PDB 2WTE · PDBe 2WTE · UniProt Q97Y88
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