Research workbench
URATE OXIDASE DI-AZIDE complex
Analyse URATE OXIDASE DI-AZIDE complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PUV
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.3
- Source
- Aspergillus flavus
- Molecule
- Uricase
- EC
- 1.7.3.3
- UniProt
- Q00511
- Ligands
- NA, AZI
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · resolution 1.3 · 1 distinct chain · 28% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uricase (EC 1.7.3.3) | protein | 295 | 28% helix, 39% strand | Q00511 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.57 | 0.79 | 24 | empty |
| 2 | 179 | 0.47 | 0.75 | 25 | AZI |
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 Q00511
- Elsewhere: RCSB PDB 4PUV · PDBe 4PUV · UniProt Q00511
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