Research workbench
Urate oxidase aza-xanthine complex under 1500 bar of argon
Analyse Urate oxidase aza-xanthine complex under 1500 bar of argon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q09
- Type
- protein
- Length
- 590 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uricase
- EC
- 1.7.3.3
- UniProt
- Q00511
- Ligands
- AZA, ACE, NA, AR
- Pockets
- 5 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uricase (EC 1.7.3.3) | protein | 295 | 28% helix, 39% strand | Q00511 |
Ligands and binding sites
- AZA · 8-azaxanthine · ligand · 4 copies · chains A, B
- ACE · Acetyl group · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- AR · Argon · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.56 | 0.79 | 21 | empty |
| 2 | 197 | 0.55 | 0.79 | 20 | empty |
| 3 | 202 | 0.54 | 0.78 | 28 | AZA |
| 4 | 190 | 0.53 | 0.78 | 28 | AZA |
| 5 | 76 | 0.31 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2744 Ų buried · 38 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 7Q09 · Urate oxidase aza-xanthine complex under 1500 bar of argon · the same entry in another collection · 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 Q00511
- Elsewhere: RCSB PDB 7Q09 · PDBe 7Q09 · UniProt Q00511
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