Annotations: 2XTS

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Cytochrome_CBB3	e2xtsB1	A: alpha arrays	X: Cytochrome c-like	H: Cytochrome c (From Topology)	T: Cytochrome c	F: Cytochrome_CBB3	ECOD (1.6)
D	Cytochrome_CBB3	e2xtsD1	A: alpha arrays	X: Cytochrome c-like	H: Cytochrome c (From Topology)	T: Cytochrome c	F: Cytochrome_CBB3	ECOD (1.6)
A	Mo-co_dimer	e2xtsA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Mo-co_dimer	ECOD (1.6)
A	Oxidored_molyb	e2xtsA2	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Sulfite oxidase, middle catalytic domain	F: Oxidored_molyb	ECOD (1.6)
C	Mo-co_dimer	e2xtsC1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Mo-co_dimer	ECOD (1.6)
C	Oxidored_molyb	e2xtsC2	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Sulfite oxidase, middle catalytic domain	F: Oxidored_molyb	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.10.760.10	Mainly Alpha	Orthogonal Bundle	Cytochrome Bc1 Complex	Chain D, domain 2	CATH (4.3.0)
D	1.10.760.10	Mainly Alpha	Orthogonal Bundle	Cytochrome Bc1 Complex	Chain D, domain 2	CATH (4.3.0)
A	3.90.420.10	Alpha Beta	Alpha-Beta Complex	Sulfite Oxidase	Chain A, domain 2	CATH (4.3.0)
A	2.60.40.650	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
C	3.90.420.10	Alpha Beta	Alpha-Beta Complex	Sulfite Oxidase	Chain A, domain 2	CATH (4.3.0)
C	2.60.40.650	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B, D	PF13442	Cytochrome C oxidase, cbb3-type, subunit III (Cytochrome_CBB3)	Cytochrome C oxidase, cbb3-type, subunit III	-	Domain
A, C	PF00174	Oxidoreductase molybdopterin binding domain (Oxidored_molyb)	Oxidoreductase molybdopterin binding domain	This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.	Domain
A, C	PF03404	Mo-co oxidoreductase dimerisation domain (Mo-co_dimer)	Mo-co oxidoreductase dimerisation domain	This domain is found in molybdopterin cofactor (Mo-co) oxidoreductases. It is involved in dimer formation, and has an Ig-fold structure [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B, D	CYTOCHROME	binding organic cyclic compound binding tetrapyrrole binding heme binding electron transfer activity cation binding ion binding metal ion binding small molecule binding	-	-
A, C	SULFITE DEHYDROGENASE	oxidoreductase activity catalytic activity cation binding transition metal ion binding molybdenum ion binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B, D	IPR036909	Cytochrome c-like domain superfamily	Homologous Superfamily
B, D	IPR009056	Cytochrome c-like domain	Domain
B, D	IPR002327	Cytochrome c, class IA/ IB	Family
A, C	IPR030835	Sulfite dehydrogenase SoxC	Family
A, C	IPR000572	Oxidoreductase, molybdopterin-binding domain	Domain
A, C	IPR014756	Immunoglobulin E-set	Homologous Superfamily
A, C	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A, C	IPR005066	Moybdenum cofactor oxidoreductase, dimerisation	Domain
A, C	IPR008335	Eukaryotic molybdopterin oxidoreductase	Family
A, C	IPR036374	Oxidoreductase, molybdopterin-binding domain superfamily	Homologous Superfamily

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.