Annotations: 1GCU

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1gcua1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain	Biliverdin reductase	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
A	d1gcua2	Alpha and beta proteins (a+b)	FwdE/GAPDH domain-like	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	Biliverdin reductase	Biliverdin reductase	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	GAPDH-like	8000942	3000043	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	PF09166	e1gcuA1	A: a+b two layers	X: FwdE/GAPDH domain-like	H: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)	T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	F: PF09166	ECOD (1.6)
A	PF01408	e1gcuA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF01408	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.30.360.10	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01408	Oxidoreductase family, NAD-binding Rossmann fold (GFO_IDH_MocA)	Oxidoreductase family, NAD-binding Rossmann fold	-	Family
A	PF09166	Biliverdin reductase, catalytic (Biliv-reduc_cat)	Biliverdin reductase, catalytic	Members of this family adopt a structure consisting of four alpha helices and six beta sheets, in an alpha-beta-alpha-alpha-alpha-beta-beta-beta-beta-beta arrangement. They contain a catalytic active site, capable of reducing the gamma-methene bridge ...	Members of this family adopt a structure consisting of four alpha helices and six beta sheets, in an alpha-beta-alpha-alpha-alpha-beta-beta-beta-beta-beta arrangement. They contain a catalytic active site, capable of reducing the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	BILIVERDIN REDUCTASE A	oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-CH group of donors catalytic activity biliverdin reductase (NADPH) activity biliverdin reductase (NAD(P)H) activity biliberdin reductase NAD+ activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-CH group of donors catalytic activity biliverdin reductase (NADPH) activity biliverdin reductase (NAD(P)H) activity biliberdin reductase NAD+ activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding	organonitrogen compound catabolic process pigment catabolic process pigment metabolic process heme metabolic process organonitrogen compound metabolic process catabolic process tetrapyrrole metabolic process organic cyclic compound catabolic process organic cyclic compound metabolic process organic substance metabolic process heme catabolic process porphyrin-containing compound catabolic process metabolic process porphyrin-containing compound metabolic process organonitrogen compound catabolic process pigment catabolic process pigment metabolic process heme metabolic process organonitrogen compound metabolic process catabolic process tetrapyrrole metabolic process organic cyclic compound catabolic process organic cyclic compound metabolic process organic substance metabolic process heme catabolic process porphyrin-containing compound catabolic process metabolic process porphyrin-containing compound metabolic process organic substance catabolic process tetrapyrrole catabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR017094	Biliverdin reductase A	Family
A	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR015249	Biliverdin reductase, catalytic	Domain
A	IPR000683	Gfo/Idh/MocA-like oxidoreductase, N-terminal	Domain

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

Chains	Enzyme Name	Description	Catalytic Residues
A	biliverdin reductase M-CSA #566	Biliverdin reductase is an evolutionarily conserved soluble protein found primarily in mammalian species. The enzyme reduces the gamma-methylene bridge of biliverdin to form bilirubin in the presence of the NAD(P)H cofactor. The reductase is also a serine/threonine kinase which is activated by oxygen radicals and traslocates into the nucleus in response to cGMP and oxidative stress. The substrate and product are immune function modulators and, based on their anti-oxidant properties, it has been suggested, although not universally accepted that biliverdin and bilirubin play a protective role in the cell.	Defined by 6 residues: GLU:A-96TYR:A-97GLU:A-123GLU:A-126SER:A-170ARG:A-171 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.3.1.24 (PDB Primary Data) Search M-CSA Motif + EC 1.3.1.24

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 R01GM133198.