Research workbench
The crystal structure of adenosine deaminase from Pseudomonas aeruginosa
Analyse The crystal structure of adenosine deaminase from Pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OU8
- Type
- protein
- Length
- 627 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.51
- Source
- Pseudomonas aeruginosa
- Molecule
- Adenosine deaminase
- EC
- 3.5.4.4
- UniProt
- Q9I6Y4
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · resolution 2.51 · 2 distinct chains · 56% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine deaminase (EC 3.5.4.4) | protein | 313 | 55% helix, 13% strand | Q9I6Y4 |
| B | Adenosine deaminase (EC 3.5.4.4) | protein | 314 | 57% helix, 13% strand | Q9I6Y4 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.45 | 0.75 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 779 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3OU8 · The crystal structure of adenosine deaminase from pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
- Q9I6Y4 · AlphaFold monomer V2.0 prediction for adenine deaminase (Q9I6Y4) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q9I6Y4
- Elsewhere: RCSB PDB 3OU8 · PDBe 3OU8 · UniProt Q9I6Y4
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