1WNW

D136N mutant of Heme Oxygenase from Corynebacterium diphtheriae (HmuO)

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
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d1wnwc_	All alpha proteins	Heme oxygenase-like	Heme oxygenase-like	Eukaryotic type heme oxygenase	Heme oxygenase HmuO	(Corynebacterium diphtheriae ) [TaxId: 1717 ],	SCOPe (2.08)
A	d1wnwa_	All alpha proteins	Heme oxygenase-like	Heme oxygenase-like	Eukaryotic type heme oxygenase	Heme oxygenase HmuO	(Corynebacterium diphtheriae ) [TaxId: 1717 ],	SCOPe (2.08)
B	d1wnwb_	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)
C	SCOP2B Superfamily	Heme oxygenase-like	8072972	3001676	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Heme oxygenase-like	8072972	3001676	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Heme oxygenase-like	8072972	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)
C	Heme_oxygenase	e1wnwC1	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)
A	Heme_oxygenase	e1wnwA1	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	e1wnwB1	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)
C	1.20.910.10	Mainly Alpha	Up-down Bundle	Heme Oxygenase	Chain A	CATH (4.3.0)
A	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	organonitrogen compound catabolic process heme metabolic process pigment metabolic process organonitrogen compound metabolic process catabolic process heme oxidation tetrapyrrole metabolic process organic cyclic compound catabolic process organic cyclic compound metabolic process organic substance metabolic process porphyrin-containing compound catabolic process metabolic process porphyrin-containing compound metabolic process organic substance catabolic process organonitrogen compound catabolic process heme metabolic process pigment metabolic process organonitrogen compound metabolic process catabolic process heme oxidation tetrapyrrole metabolic process organic cyclic compound catabolic process organic cyclic compound metabolic process organic substance metabolic process porphyrin-containing compound catabolic process metabolic process porphyrin-containing compound metabolic process organic substance catabolic 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

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
B	heme oxygenase (biliverdin-producing) M-CSA #795	Heme oxygenase (HO) catalyses the breakdown of heme to release biliverdin, CO, and free iron, and is found in mammals, plants and photosynthetic bacteria. The roles of the heme catabolism process are different in mammals and plants: whilst mammals use HO to degrade excess heme from red blood cells, plants and cyanobacteria use HO activity in order to generate the biliverdin needed for the production of light harvesting complexes. As a result, their is little sequence or structural homology between the mammalian and other forms, indicating that they may have evolved independently. However, the reaction seems to proceed via the same mechanism in both, with key active site residues being the same between the two groups. The bacterial form is described here, but the catalytic residues are the same in both the mammalian and plant forms of the enzyme.	Defined by 7 residues: HIS:B-25TYR:B-53VAL:B-131ARG:B-132GLY:B-135ASN:B-136GLY:B-140 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.14.99.3 (PDB Primary Data) Search M-CSA Motif + EC 1.14.99.3

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.