1KBV

NITRITE-SOAKED CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF ANIA FROM NEISSERIA GONORRHOEAE

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)
A	d1kbva2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, C-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
A	d1kbva1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, N-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
B	d1kbvb2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, C-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
B	d1kbvb1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, N-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
C	d1kbvc2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, C-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
C	d1kbvc1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, N-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
D	d1kbvd2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, C-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
D	d1kbvd1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, N-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
E	d1kbve2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, C-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
E	d1kbve1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, N-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
F	d1kbvf2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, C-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)
F	d1kbvf1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, N-terminal domain	(Neisseria gonorrhoeae ) [TaxId: 485 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Multidomain cupredoxins	8025623	4002203	SCOP2 (2022-06-29)
A	SCOP2 Family	Multidomain cupredoxins	8025624	4002203	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Cupredoxins	8038002	3000886	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Cupredoxins	8038003	3000886	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Cupredoxins	8038002	3000886	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cupredoxins	8038003	3000886	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Cupredoxins	8038003	3000886	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Cupredoxins	8038002	3000886	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Cupredoxins	8038002	3000886	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Cupredoxins	8038003	3000886	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Cupredoxins	8038002	3000886	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Cupredoxins	8038003	3000886	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Cupredoxins	8038002	3000886	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Cupredoxins	8038003	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_2	e1kbvA2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2_2	ECOD (1.6)
A	Cu-oxidase_3_1	e1kbvA1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	ECOD (1.6)
B	Cu-oxidase_2_2	e1kbvB2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2_2	ECOD (1.6)
B	Cu-oxidase_3_1	e1kbvB1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	ECOD (1.6)
C	Cu-oxidase_2_2	e1kbvC2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2_2	ECOD (1.6)
C	Cu-oxidase_3_1	e1kbvC1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	ECOD (1.6)
D	Cu-oxidase_2_2	e1kbvD2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2_2	ECOD (1.6)
D	Cu-oxidase_3_1	e1kbvD1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	ECOD (1.6)
E	Cu-oxidase_2_2	e1kbvE2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2_2	ECOD (1.6)
E	Cu-oxidase_3_1	e1kbvE1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	ECOD (1.6)
F	Cu-oxidase_2_2	e1kbvF2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2_2	ECOD (1.6)
F	Cu-oxidase_3_1	e1kbvF1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	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)
B	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)
C	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)
D	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)
E	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)
F	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, B, C, D, E A, B, C, D, E, F	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Major outer membrane protein PAN 1	cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity, acting on other nitrogenous compounds as donors, cytochrome as acceptor oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors nitrite reductase (NO-forming) activity nitrite reductase activity catalytic activity	-	cell periphery cell outer membrane cellular anatomical structure external encapsulating structure membrane cell envelope outer membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR008972	Cupredoxin	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR045087	Multicopper oxidase	Family
A, B, C, D, E A, B, C, D, E, F	IPR001287	Nitrite reductase, copper-type	Family
A, B, C, D, E A, B, C, D, E, F	IPR011707	Multicopper oxidase-like, N-terminal	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.