4US8

Aldehyde Oxidoreductase from Desulfovibrio gigas (MOP), soaked with benzaldehyde

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
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4us8a2	All alpha proteins	CO dehydrogenase ISP C-domain like	CO dehydrogenase ISP C-domain like	CO dehydrogenase ISP C-domain like	Aldehyde oxidoreductase, domain 2	(Megalodesulfovibrio gigas ) [TaxId: 879 ],	SCOPe (2.08)
A	d4us8a1	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	2Fe-2S ferredoxin-like	2Fe-2S ferredoxin domains from multidomain proteins	Aldehyde oxidoreductase, N-terminal domain	(Megalodesulfovibrio gigas ) [TaxId: 879 ],	SCOPe (2.08)
A	d4us8a3	Alpha and beta proteins (a+b)	alpha/beta-Hammerhead	CO dehydrogenase molybdoprotein N-domain-like	CO dehydrogenase molybdoprotein N-domain-like	Aldehyde oxidoreductase, domain 3	(Megalodesulfovibrio gigas ) [TaxId: 879 ],	SCOPe (2.08)
A	d4us8a4	Alpha and beta proteins (a+b)	Molybdenum cofactor-binding domain	Molybdenum cofactor-binding domain	Molybdenum cofactor-binding domain	Aldehyde oxidoreductase	(Megalodesulfovibrio gigas ) [TaxId: 879 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Molybdenum cofactor-binding domain	8041445	3000625	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CO dehydrogenase molybdoprotein N-domain-like	8041443	3000847	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	2Fe-2S ferredoxin-like	8041442	3000113	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CO dehydrogenase ISP C-domain like	8041441	3000439	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	Fer2_2	e4us8A3	A: alpha bundles	X: CO dehydrogenase ISP C-domain like (From Topology)	H: CO dehydrogenase ISP C-domain like (From Topology)	T: CO dehydrogenase ISP C-domain like	F: Fer2_2	ECOD (1.6)
A	Fer2	e4us8A2	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: Fer2	ECOD (1.6)
A	Ald_Xan_dh_C2	e4us8A5	A: a+b two layers	X: MocoBD/DmpA-related (From Homology)	H: MocoBD/DmpA-related	T: Molybdenum cofactor-binding domain	F: Ald_Xan_dh_C2	ECOD (1.6)
A	Ald_Xan_dh_C	e4us8A1	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: alpha/beta-Hammerhead/Barrel-sandwich hybrid	T: CO dehydrogenase molybdoprotein N-domain-like	F: Ald_Xan_dh_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.20.30	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Beta-grasp domain	CATH (4.3.0)
A	1.10.150.120	Mainly Alpha	Orthogonal Bundle	DNA polymerase	domain 1	CATH (4.3.0)
A	3.90.1170.50	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
A	3.30.365.10	Alpha Beta	2-Layer Sandwich	Aldehyde Oxidoreductase	domain 4	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01799	[2Fe-2S] binding domain (Fer2_2)	[2Fe-2S] binding domain	-	Domain
A	PF01315	Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain (Ald_Xan_dh_C)	Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain	-	Domain
A	PF20256	Molybdopterin cofactor-binding domain (MoCoBD_2)	Molybdopterin cofactor-binding domain	-	Domain
A	PF02738	Molybdopterin cofactor-binding domain (MoCoBD_1)	Molybdopterin cofactor-binding domain	-	Domain
A	PF00111	2Fe-2S iron-sulfur cluster binding domain (Fer2)	2Fe-2S iron-sulfur cluster binding domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ALDEHYDE OXIDOREDUCTASE	iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding binding metal cluster binding small molecule binding oxidoreductase activity aldehyde dehydrogenase (FAD-independent) activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity cation binding transition metal ion binding iron ion binding ion binding metal ion binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR054705	Molybdopterin-dependent aldehyde oxidoreductase	Family
A	IPR036010	2Fe-2S ferredoxin-like superfamily	Homologous Superfamily
A	IPR000674	Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead	Domain
A	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain	Domain
A	IPR006058	2Fe-2S ferredoxin, iron-sulphur binding site	Binding Site
A	IPR036856	Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead superfamily	Homologous Superfamily
A	IPR037165	Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain superfamily	Homologous Superfamily
A	IPR046867	Aldehyde oxidase/xanthine dehydrogenase, second molybdopterin binding domain	Domain
A	IPR002888	[2Fe-2S]-binding	Domain
A	IPR036884	[2Fe-2S]-binding domain superfamily	Homologous Superfamily
A	IPR016208	Aldehyde oxidase/xanthine dehydrogenase-like	Family
A	IPR012675	Beta-grasp domain superfamily	Homologous Superfamily
A	IPR008274	Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	CSO	Parent Component: CYS RESID: AA0205 PSI-MOD : L-cysteine sulfenic acid MOD:00210

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.