1WX2

Crystal Structure of the oxy-form of the copper-bound Streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein prepared by the addition of hydrogenperoxide

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1wx2b_	Alpha and beta proteins (a+b)	Tyrosinase cofactor MelC1-like	Tyrosinase cofactor MelC1	Tyrosinase cofactor MelC1	Tyrosinase cofactor MelC1	(Streptomyces castaneoglobisporus ) [TaxId: 79261 ],	SCOPe (2.08)
A	d1wx2a1	All alpha proteins	Di-copper centre-containing domain	Di-copper centre-containing domain	Tyrosinase	Tyrosinase	(Streptomyces castaneoglobisporus ) [TaxId: 79261 ],	SCOPe (2.08)
A	d1wx2a2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Streptomyces castaneoglobisporus ) [TaxId: 79261 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Tyrosinase-specific caddie protein-like	8107026	3002870	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)
B	MelC1	e1wx2B1	A: a+b two layers	X: SH2 (From Topology)	H: SH2 (From Topology)	T: SH2	F: MelC1	ECOD (1.6)
A	Tyrosinase	e1wx2A1	A: alpha arrays	X: Di-copper centre-containing domain (From Topology)	H: Di-copper centre-containing domain (From Topology)	T: Di-copper centre-containing domain	F: Tyrosinase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.1880.10	Alpha Beta	2-Layer Sandwich	protein ne1242 fold	protein ne1242 domain like	CATH (4.3.0)
A	1.10.1280.10	Mainly Alpha	Orthogonal Bundle	di-copper center containing domain from catechol oxidase	Di-copper center containing domain from catechol oxidase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00264	Common central domain of tyrosinase (Tyrosinase)	Common central domain of tyrosinase	This family also contains polyphenol oxidases and some hemocyanins. Binds two copper ions via two sets of three histidines. This family is related to Pfam:PF00372.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B	MelC	cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding	pigment metabolic process organic hydroxy compound metabolic process pigment biosynthetic process melanin metabolic process secondary metabolic process biosynthetic process secondary metabolite biosynthetic process organic hydroxy compound biosynthetic process phenol-containing compound metabolic process phenol-containing compound biosynthetic process metabolic process melanin biosynthetic process	-
A	tyrosinase	oxidoreductase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B	IPR023199	Copper chaperone GriE/MELC1 superfamily	Homologous Superfamily
B	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
B	IPR010928	Tyrosinase co-factor MelC1	Family
A	IPR008922	Di-copper centre-containing domain superfamily	Homologous Superfamily
A	IPR050316	Tyrosinase and Hemocyanin	Family
A	IPR002227	Tyrosinase copper-binding domain	Domain

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.