4AKO

Mutations in the neighbourhood of CotA-laccase trinuclear site: E498L mutant

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	d4akoa1	All beta proteins	Cupredoxin-like	Cupredoxins	automated matches	automated matches	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cupredoxins	8032944	3000886	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Cupredoxins	8032945	3000886	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Cupredoxins	8032943	3000886	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	Cu-oxidase_2	e4akoA3	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2	ECOD (1.6)
A	Cu-oxidase_3_1	e4akoA6	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	ECOD (1.6)
A	Cu-oxidase	e4akoA2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00394	Multicopper oxidase (Cu-oxidase)	Multicopper oxidase	Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.	Domain
A	PF07732	Multicopper oxidase (Cu-oxidase_3)	Multicopper oxidase	This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model.	Domain
A	PF07731	Multicopper oxidase (Cu-oxidase_2)	Multicopper oxidase	This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	SPORE COAT PROTEIN A	oxidoreductase activity catalytic activity cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding	sporulation resulting in formation of a cellular spore developmental process anatomical structure morphogenesis anatomical structure formation involved in morphogenesis anatomical structure development sporulation	outer membrane-bounded periplasmic space cell envelope periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR008972	Cupredoxin	Homologous Superfamily
A	IPR001117	Multicopper oxidase, second cupredoxin domain	Domain
A	IPR011706	Multicopper oxidase, C-terminal	Domain
A	IPR045087	Multicopper oxidase	Family
A	IPR011707	Multicopper oxidase-like, N-terminal	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	CSX	Parent Component: CYS RESID: AA0451 PSI-MOD : 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide MOD:01380

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.