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Urate oxidase from aspergillus flavus complexed with its inhibitor 9- methyl uric acid

Analyse Urate oxidase from aspergillus flavus complexed with its inhibitor 9- methyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1R4S
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
CYS, MUA
Pockets
2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUricase (EC 1.7.3.3)protein29528% helix, 38% strandQ00511

Ligands and binding sites

  • CYS · Cysteine · ligand · chains A
  • MUA · 9-methyl uric acid · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12200.560.7823empty
21870.470.7523MUA

Modifications

Observed in the structure: 1 covalent, 1 modified (covalent ligand, acetylation).

Compared structures

  • 1R4S · Urate oxidase from aspergillus flavus complexed with its inhibitor 9-methyl uric acid · the same entry in another collection · chain A against A, TM-score 1.00
  • Q00511 · AlphaFold monomer V2.0 prediction for uricase (Q00511) · a predicted model of the same protein · chain A against A, TM-score 0.99

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