Research workbench
Urate oxidase from aspergillus flavus complexed with 5-amino 6-nitro uracil
Analyse Urate oxidase from aspergillus flavus complexed with 5-amino 6-nitro uracil in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WRR
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uricase
- EC
- 1.7.3.3
- UniProt
- Q00511
- Ligands
- UNC
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 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
- UNC · 5-amino-6-nitropyrimidine-2,4(1H,3H)-dione · ligand · chains A
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 | 210 | 0.56 | 0.79 | 21 | empty |
| 2 | 179 | 0.46 | 0.75 | 23 | UNC |
Modifications
Observed in the structure: 1 modified (acetylation).
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 1WRR · PDBe 1WRR · UniProt Q00511
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