Research workbench
Crystal structure of CAS1 from archaeoglobus fulgidus and its nucleolytic activity
Analyse Crystal structure of CAS1 from archaeoglobus fulgidus and its nucleolytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N06
- Type
- protein
- Length
- 693 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated endonuclease CAS1 1
- EC
- 3.1.-.-
- UniProt
- O28401
- Pockets
- 9 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated endonuclease CAS1 1 (EC 3.1.-.-) | protein | 346 | 52% helix, 17% strand | O28401 |
| B | CRISPR-associated endonuclease CAS1 1 (EC 3.1.-.-) | protein | 347 | 52% helix, 17% strand | O28401 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1166 | 0.86 | 0.87 | 106 | empty |
| 2 | 141 | 0.63 | 0.86 | 26 | empty |
| 3 | 313 | 0.61 | 0.78 | 32 | empty |
| 4 | 125 | 0.49 | 0.80 | 24 | empty |
| 5 | 115 | 0.42 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1289 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 4N06 · Crystal structure of Cas1 from Archaeoglobus fulgidus and its nucleolytic activity · the same entry in another collection · chain A against A, TM-score 1.00
- O28401 · AlphaFold monomer V2.0 prediction for CRISPR-associated endonuclease CAS1 1 (O28401) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 O28401
- Elsewhere: RCSB PDB 4N06 · PDBe 4N06 · UniProt O28401
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