4UHX
Human aldehyde oxidase in complex with phthalazine and thioridazine
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | Fer2_2 | e4uhxA1 | 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 | e4uhxA4 | A: a+b two layers | X: beta-Grasp | H: Ubiquitin-related | T: Ubiquitin-like | F: Fer2 | ECOD (1.6) |
A | Ald_Xan_dh_C2 | e4uhxA3 | 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 | CO_deh_flav_C | e4uhxA5 | A: a+b two layers | X: FAD-linked reductases, C-terminal domain-like | H: SufE/NifU (From Topology) | T: SufE/NifU | F: CO_deh_flav_C | ECOD (1.6) |
A | FAD_binding_5 | e4uhxA2 | A: a+b complex topology | X: FAD-binding domain-like | H: FAD-binding domain (From Topology) | T: FAD-binding domain | F: FAD_binding_5 | ECOD (1.6) |
A | Ald_Xan_dh_C | e4uhxA6 | 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 (utative) |
A | 1.10.150.120 | Mainly Alpha | Orthogonal Bundle | DNA polymerase | domain 1 | CATH (utative) |
A | 3.30.43.10 | Alpha Beta | 2-Layer Sandwich | Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase | domain 2 | CATH (utative) |
A | 3.30.390.50 | Alpha Beta | 2-Layer Sandwich | Enolase-like | domain 1 | CATH (utative) |
A | 3.30.365.10 | Alpha Beta | 2-Layer Sandwich | Aldehyde Oxidoreductase | domain 4 | CATH (utative) |
A | 3.90.1170.50 | Alpha Beta | Alpha-Beta Complex | Aldehyde Oxidoreductase | domain 3 | CATH (utative) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00941 | FAD binding domain in molybdopterin dehydrogenase (FAD_binding_5) | FAD binding domain in molybdopterin dehydrogenase | - | Family | |
PF01799 | [2Fe-2S] binding domain (Fer2_2) | [2Fe-2S] binding domain | - | Domain | |
PF01315 | Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain (Ald_Xan_dh_C) | Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain | - | Domain | |
PF20256 | Molybdopterin cofactor-binding domain (MoCoBD_2) | Molybdopterin cofactor-binding domain | - | Domain | |
PF03450 | CO dehydrogenase flavoprotein C-terminal domain (CO_deh_flav_C) | CO dehydrogenase flavoprotein C-terminal domain | - | Domain | |
PF02738 | Molybdopterin cofactor-binding domain (MoCoBD_1) | Molybdopterin cofactor-binding domain | - | Domain | |
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
InterPro: Protein Family Classification InterPro Database Homepage
Pharos: Disease Associations Pharos Homepage Annotation
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
aldehyde oxidase M-CSA #968 | Aldehyde oxidase is a member of the xanthine oxidase family. It is a complex molybdoenzyme containing a Mo cofactor (Moco), flavin adenine nucleotide (FAD) and two Fe2S2 clusters. The enzyme has broad substrate specificity and catalyses a wide range of reactions. This includes the oxidation of aldehydes and several N-heterocycles, as well as the reduction of some substrates. In the human liver, the enzyme plays an essential role in the detoxification of xenobiotics and contributes to the hepatic clearance of many other drugs. | EC: 1.2.3.1 (PDB Primary Data) EC: 1.17.3 (UniProt) |