MolNFT v1 · #76891 · protein
Crystal structure of the CRISPR-associated protein SSO1393 from sulfolobus solfataricus
3QYF: “Crystal structure of the CRISPR-associated protein SSO1393 from sulfolobus solfataricus”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.66). MolNFT v1 #76891 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 3QYF
- Type
- protein
- Length
- 541 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated protein
- UniProt
- Q97YD2
- Ligands
- MG
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated protein | protein | 271 | 54% helix, 19% strand | Q97YD2 |
| B | CRISPR-associated protein | protein | 270 | 53% helix, 19% strand | Q97YD2 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 556 | 0.66 | 0.77 | 62 | empty |
| 2 | 266 | 0.60 | 0.79 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 2215 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 3QYF · Crystal structure of the CRISPR-associated protein SSO1393 from Sulfolobus solfataricus · the same entry in another collection · chain A against A, TM-score 1.00
- Q97YD2 · AlphaFold monomer V2.0 prediction for CRISPR system ring nuclease SSO1393 (Q97YD2) · 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 Q97YD2
- Elsewhere: RCSB PDB 3QYF · PDBe 3QYF · UniProt Q97YD2
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