3W6Q | pdb_00003w6q

Crystal structure of melB apo-protyrosinase from Asperugillus oryzae

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EUF07665	e3w6qA2	A: beta sandwiches	X: jelly-roll	H: C-terminal domain of mullusc hemocyanin (From Topology)	T: C-terminal domain of mullusc hemocyanin	F: EUF07665	ECOD (1.6)
A	Tyrosinase	e3w6qA1	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)
B	EUF07665	e3w6qB2	A: beta sandwiches	X: jelly-roll	H: C-terminal domain of mullusc hemocyanin (From Topology)	T: C-terminal domain of mullusc hemocyanin	F: EUF07665	ECOD (1.6)
B	Tyrosinase	e3w6qB1	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)
C	EUF07665	e3w6qC2	A: beta sandwiches	X: jelly-roll	H: C-terminal domain of mullusc hemocyanin (From Topology)	T: C-terminal domain of mullusc hemocyanin	F: EUF07665	ECOD (1.6)
C	Tyrosinase	e3w6qC1	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)
D	EUF07665	e3w6qD2	A: beta sandwiches	X: jelly-roll	H: C-terminal domain of mullusc hemocyanin (From Topology)	T: C-terminal domain of mullusc hemocyanin	F: EUF07665	ECOD (1.6)
D	Tyrosinase	e3w6qD3	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)
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)
A	2.60.310.20	Mainly Beta	Sandwich	Hemocyanin	Chain: A, domain 2	CATH (4.3.0)
B	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)
B	2.60.310.20	Mainly Beta	Sandwich	Hemocyanin	Chain: A, domain 2	CATH (4.3.0)
C	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)
C	2.60.310.20	Mainly Beta	Sandwich	Hemocyanin	Chain: A, domain 2	CATH (4.3.0)
D	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)
D	2.60.310.20	Mainly Beta	Sandwich	Hemocyanin	Chain: A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF18132	Tyrosinase C-terminal domain (Tyrosinase_C)	Tyrosinase C-terminal domain	This is the C-terminal domain of Tyrosinase present in Aspergillus oryzae. Tyrosinase is a dinuclear copper monooxygenase/oxidase that plays a crucial role in the melanin pigment biosynthesis. The C-terminal domain is referred to as the shielding dom ...	This is the C-terminal domain of Tyrosinase present in Aspergillus oryzae. Tyrosinase is a dinuclear copper monooxygenase/oxidase that plays a crucial role in the melanin pigment biosynthesis. The C-terminal domain is referred to as the shielding domain as it prohibits substrate access to the enzyme-active site and blocks the oxidase/oxygenase activity to avoid undesirable intracellular reactions of highly reactive quinonoid products. This means the domain may play an important role in regulating the enzyme activity. Two of the three cysteines (Cys522, and Cys525) that play a significant role in the copper incorporation process belong to the C-terminal domain [1].	Domain
A, B, C, D	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
A, B, C, D	tyrosinase	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, another compound as one donor, and incorporation of one atom of oxygen oxidoreductase activity monooxygenase activity tyrosinase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen catalytic activity cation binding ion binding binding metal ion binding small molecule binding	pigment metabolic process pigment biosynthetic process melanin metabolic process secondary metabolic process biosynthetic process secondary metabolite biosynthetic process phenol-containing compound metabolic process phenol-containing compound biosynthetic process metabolic process cellular process melanin biosynthetic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR008922	Di-copper centre-containing domain superfamily	Homologous Superfamily
A, B, C, D	IPR015021	Ester hydrolase C11orf54, Domain of unknown function DUF1907	Domain
A, B, C, D	IPR041640	Tyrosinase, C-terminal	Domain
A, B, C, D	IPR050316	Tyrosinase and Hemocyanin	Family
A, B, C, D	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.