4GPH

Structure of HmuO, heme oxygenase from Corynebacterium diphtheriae, in complex with the putative reaction intermediates between Fe3+-biliverdin and biliverdin (data set IV)

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	d4gpha_	All alpha proteins	Heme oxygenase-like	Heme oxygenase-like	Eukaryotic type heme oxygenase	Heme oxygenase HmuO	(Corynebacterium diphtheriae ) [TaxId: 1717 ],	SCOPe (2.08)
C	d4gphc_	All alpha proteins	Heme oxygenase-like	Heme oxygenase-like	Eukaryotic type heme oxygenase	Heme oxygenase HmuO	(Corynebacterium diphtheriae ) [TaxId: 1717 ],	SCOPe (2.08)
B	d4gphb_	All alpha proteins	Heme oxygenase-like	Heme oxygenase-like	Eukaryotic type heme oxygenase	Heme oxygenase HmuO	(Corynebacterium diphtheriae ) [TaxId: 1717 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Heme oxygenase-like	8038222	3001676	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Heme oxygenase-like	8038222	3001676	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Heme oxygenase-like	8038222	3001676	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	Heme_oxygenase	e4gphA1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Heme oxygenase/Ribonucleotide reductase	F: Heme_oxygenase	ECOD (1.6)
C	Heme_oxygenase	e4gphC1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Heme oxygenase/Ribonucleotide reductase	F: Heme_oxygenase	ECOD (1.6)
B	Heme_oxygenase	e4gphB1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Heme oxygenase/Ribonucleotide reductase	F: Heme_oxygenase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.910.10	Mainly Alpha	Up-down Bundle	Heme Oxygenase	Chain A	CATH (4.3.0)
C	1.20.910.10	Mainly Alpha	Up-down Bundle	Heme Oxygenase	Chain A	CATH (4.3.0)
B	1.20.910.10	Mainly Alpha	Up-down Bundle	Heme Oxygenase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF01126	Heme oxygenase (Heme_oxygenase)	Heme oxygenase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Heme oxygenase	oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen heme oxygenase (decyclizing) activity catalytic activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen cation binding ion binding binding metal ion binding small molecule binding	heme metabolic process pigment metabolic process catabolic process heme oxidation tetrapyrrole metabolic process porphyrin-containing compound catabolic process metabolic process cellular process porphyrin-containing compound metabolic process tetrapyrrole catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR018207	Haem oxygenase conserved site	Conserved Site
A, B, C	IPR002051	Haem oxygenase	Family
A, B, C	IPR016084	Haem oxygenase-like, multi-helical	Homologous Superfamily
A, B, C	IPR016053	Haem oxygenase-like	Family

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.