3DWS

Leishmania major Coproporphyrinogen III Oxidase with bound ligand

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	d3dwsa2	Alpha and beta proteins (a+b)	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	automated matches	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
A	d3dwsa3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
B	d3dwsb2	Alpha and beta proteins (a+b)	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	Coproporphyrinogen III oxidase	automated matches	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
B	d3dwsb3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Coproporphyrinogen III oxidase	8036379	3001418	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Coproporphyrinogen III oxidase	8036379	3001418	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	Coprogen_oxidas	e3dwsA1	A: a+b three layers	X: Coproporphyrinogen III oxidase (From Topology)	H: Coproporphyrinogen III oxidase (From Topology)	T: Coproporphyrinogen III oxidase	F: Coprogen_oxidas	ECOD (1.6)
B	Coprogen_oxidas	e3dwsB1	A: a+b three layers	X: Coproporphyrinogen III oxidase (From Topology)	H: Coproporphyrinogen III oxidase (From Topology)	T: Coproporphyrinogen III oxidase	F: Coprogen_oxidas	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1500.10	Alpha Beta	3-Layer(aba) Sandwich	oxygen-dependent coproporphyrinogen oxidase	Coproporphyrinogen III oxidase, aerobic	CATH (4.3.0)
B	3.40.1500.10	Alpha Beta	3-Layer(aba) Sandwich	oxygen-dependent coproporphyrinogen oxidase	Coproporphyrinogen III oxidase, aerobic	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01218	Coproporphyrinogen III oxidase (Coprogen_oxidas)	Coproporphyrinogen III oxidase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Coproporphyrinogen III oxidase	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity oxidoreductase activity coproporphyrinogen oxidase activity oxidoreductase activity, acting on the CH-CH group of donors catalytic activity oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor	pigment metabolic process heme metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process protoporphyrinogen IX metabolic process pigment biosynthetic process protoporphyrinogen IX biosynthetic process tetrapyrrole biosynthetic process biosynthetic process metabolic process porphyrin-containing compound metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036406	Oxygen-dependent coproporphyrinogen III oxidase superfamily	Homologous Superfamily
A, B	IPR001260	Coproporphyrinogen III oxidase, aerobic	Family
A, B	IPR018375	Coproporphyrinogen III oxidase, conserved site	Conserved Site

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.