Research workbench
Urate oxydase aza-xanthine complex at 1000 bars (100 mpa) of argon
Analyse Urate oxydase aza-xanthine complex at 1000 bars (100 mpa) of argon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PWN
- 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
- ACE, AZA, NA, AR
- Pockets
- 6 · best druggability 0.57
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
- ACE · Acetyl group · ligand · 2 copies · chains A, B
- AZA · 8-azaxanthine · 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
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.57 | 0.79 | 22 | empty |
| 2 | 198 | 0.56 | 0.79 | 22 | empty |
| 3 | 197 | 0.53 | 0.78 | 30 | AZA |
| 4 | 161 | 0.49 | 0.77 | 22 | AZA |
| 5 | 75 | 0.30 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2728 Ų buried · 40 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 7PWN · URATE OXYDASE AZA-XANTHINE COMPLEX AT 1000 BARS (100 MPa) 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 7PWN · PDBe 7PWN · UniProt Q00511
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