Research workbench
The structure of the CRISPR-associated protein, CSA2, from sulfolobus solfataricus
Analyse The structure of the CRISPR-associated protein, CSA2, from sulfolobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PS0
- Type
- protein
- Length
- 1,129 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated protein, CSA2
- UniProt
- Q97Y91
- Pockets
- 10 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated protein, CSA2 | protein | 293 | 38% helix, 25% strand | Q97Y91 |
| B | CRISPR-associated protein, CSA2 | protein | 272 | 36% helix, 26% strand | Q97Y91 |
| C | CRISPR-associated protein, CSA2 | protein | 292 | 36% helix, 24% strand | Q97Y91 |
| D | CRISPR-associated protein, CSA2 | protein | 272 | 36% helix, 25% strand | Q97Y91 |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1110 | 0.76 | 0.78 | 103 | empty |
| 2 | 928 | 0.75 | 0.78 | 61 | empty |
| 3 | 213 | 0.55 | 0.78 | 34 | empty |
| 4 | 93 | 0.47 | 0.81 | 19 | empty |
| 5 | 143 | 0.47 | 0.77 | 22 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1595 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 1341 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 555 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 377 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 109 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3PS0 · The structure of the CRISPR-associated protein, csa2, from Sulfolobus solfataricus · the same entry in another collection · chain D against D, TM-score 1.00
- Q97Y91 · AlphaFold monomer V2.0 prediction for CRISPR-associated acascade subunit CAS7/CSA2 2… · a predicted model of the same protein · chain B against A, TM-score 0.93
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 Q97Y91
- Elsewhere: RCSB PDB 3PS0 · PDBe 3PS0 · UniProt Q97Y91
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