Research workbench
Crystal structure of S. pyogenes CAS9
Analyse Crystal structure of S. pyogenes CAS9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CMP
- Type
- protein
- Length
- 2,310 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated endonuclease CAS9/CSN1
- EC
- 3.1.-.-
- UniProt
- Q99ZW2
- Ligands
- MG, SO4
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated endonuclease CAS9/CSN1 (EC 3.1.-.-) | protein | 1144 | 52% helix, 11% strand | Q99ZW2 |
| B | CRISPR-associated endonuclease CAS9/CSN1 (EC 3.1.-.-) | protein | 1166 | 51% helix, 11% strand | Q99ZW2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 640 | 0.77 | 0.83 | 76 | SO4 |
| 2 | 767 | 0.77 | 0.81 | 70 | SO4 |
| 3 | 421 | 0.76 | 0.86 | 33 | empty |
| 4 | 511 | 0.73 | 0.82 | 57 | empty |
| 5 | 904 | 0.72 | 0.76 | 74 | empty |
Interfaces
1 interface between chains.
- A–B · 675 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 Q99ZW2
- Elsewhere: RCSB PDB 4CMP · PDBe 4CMP · UniProt Q99ZW2
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