Research workbench
Crystal structure of uncharacterized conserved protein from aquifex aeolicus
Analyse Crystal structure of uncharacterized conserved protein from aquifex aeolicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YZS
- Type
- protein
- Length
- 617 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein
- UniProt
- O66692
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein | protein | 308 | 55% helix, 18% strand | O66692 |
| B | Putative uncharacterized protein | protein | 309 | 53% helix, 17% strand | O66692 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 540 | 0.79 | 0.86 | 46 | empty |
| 2 | 300 | 0.60 | 0.78 | 37 | empty |
| 3 | 156 | 0.45 | 0.75 | 22 | empty |
| 4 | 87 | 0.37 | 0.75 | 19 | empty |
| 5 | 80 | 0.36 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1664 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2YZS · Crystal structure of uncharacterized conserved protein from Aquifex aeolicus · the same entry in another collection · chain A against A, TM-score 1.00
- O66692 · AlphaFold monomer V2.0 prediction for CRISPR-associated endonuclease CAS1 (O66692) · 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 O66692
- Elsewhere: RCSB PDB 2YZS · PDBe 2YZS · UniProt O66692
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