4PR8

URATE OXIDASE AZIDE URIC ACID TERNARY complex

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4pr8a1	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	Urate oxidase (uricase)	Urate oxidase (uricase)	(Aspergillus flavus ) [TaxId: 5059 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8042648	3000283	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8042645	3000283	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Uricase	e4pr8A1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: Uricase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.270.10	Alpha Beta	Roll	Urate Oxidase	Urate Oxidase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01014	Uricase (Uricase)	Uricase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Uricase	oxidoreductase activity urate oxidase activity oxidoreductase activity, acting on other nitrogenous compounds as donors oxidoreductase activity, acting on other nitrogenous compounds as donors, oxygen as acceptor catalytic activity	catabolic process urate catabolic process small molecule metabolic process metabolic process cellular process purine-containing compound catabolic process small molecule catabolic process purine-containing compound metabolic process urate metabolic process purine nucleobase metabolic process primary metabolic process purine nucleobase catabolic process nucleobase-containing compound metabolic process nucleobase catabolic process catabolic process urate catabolic process small molecule metabolic process metabolic process cellular process purine-containing compound catabolic process small molecule catabolic process purine-containing compound metabolic process urate metabolic process purine nucleobase metabolic process primary metabolic process purine nucleobase catabolic process nucleobase-containing compound metabolic process nucleobase catabolic process nucleobase-containing small molecule metabolic process nucleobase metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle peroxisome microbody cytoplasm intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR019842	Uricase, conserved site	Conserved Site
A	IPR002042	Uricase	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	ACE	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 PSI-MOD : N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.