Research workbench
Crystal structure of a CRISPR-associated protein from thermus thermophilus
Analyse Crystal structure of a CRISPR-associated protein from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WJ9
- Type
- protein
- Length
- 188 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated protein
- UniProt
- Q53WG9
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated protein | protein | 188 | 28% helix, 32% strand | Q53WG9 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.40 | 0.77 | 27 | empty |
| 2 | 110 | 0.39 | 0.75 | 22 | empty |
Compared structures
- 1WJ9 · Crystal structure of a CRISPR-associated protein from thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
- Q53WG9 · AlphaFold monomer V2.0 prediction for CRISPR-associated endoribonuclease CSE3 (Q53WG9) · a predicted model of the same protein · chain A 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 Q53WG9
- Elsewhere: RCSB PDB 1WJ9 · PDBe 1WJ9 · UniProt Q53WG9
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