Research workbench
Crystal structure of the CAS1-CAS2 complex from escherichia COLI
Analyse Crystal structure of the CAS1-CAS2 complex from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P6I
- Type
- protein
- Length
- 1,291 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated endoribonuclease CAS2; CRISPR-associated endonuclease CAS1
- EC
- 3.1.-.-
- UniProt
- P45956, Q46896
- Pockets
- 18 · best druggability 0.77
Structure
x-ray diffraction · 6 distinct chains · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated endoribonuclease CAS2 (EC 3.1.-.-) | protein | 101 | 27% helix, 43% strand | P45956 |
| B | CRISPR-associated endoribonuclease CAS2 (EC 3.1.-.-) | protein | 97 | 25% helix, 43% strand | P45956 |
| C | CRISPR-associated endonuclease CAS1 (EC 3.1.-.-) | protein | 270 | 53% helix, 12% strand | Q46896 |
| D | CRISPR-associated endonuclease CAS1 (EC 3.1.-.-) | protein | 288 | 49% helix, 14% strand | Q46896 |
| E | CRISPR-associated endonuclease CAS1 (EC 3.1.-.-) | protein | 259 | 52% helix, 15% strand | Q46896 |
| F | CRISPR-associated endonuclease CAS1 (EC 3.1.-.-) | protein | 276 | 54% helix, 15% strand | Q46896 |
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 244 | 0.77 | 0.90 | 35 | empty |
| 2 | 221 | 0.76 | 0.90 | 32 | empty |
| 3 | 356 | 0.61 | 0.77 | 58 | empty |
| 4 | 335 | 0.61 | 0.78 | 51 | empty |
| 5 | 290 | 0.60 | 0.79 | 43 | empty |
Interfaces
9 interfaces between chains.
- E–F · 1704 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1691 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 1222 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1121 Ų buried · 2 hydrogen bonds · protein-protein
- A–F · 867 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4P6I · Crystal structure of the Cas1-Cas2 complex from Escherichia coli · the same entry in another collection · chain F against F, TM-score 1.00
- Q46896 · AlphaFold monomer V2.0 prediction for CRISPR-associated endonuclease CAS1 (Q46896) · a predicted model of the same protein · chain F against A, TM-score 0.96
- P45956 · AlphaFold monomer V2.0 prediction for CRISPR-associated endoribonuclease CAS2 (P45956) · a predicted model of the same protein · chain B against A, TM-score 0.88
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 P45956
- Every structure of UniProt Q46896
- Elsewhere: RCSB PDB 4P6I · PDBe 4P6I · UniProt P45956 · UniProt Q46896
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