1GOG

NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE

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)
A	d1goga1	All beta proteins	Immunoglobulin-like beta-sandwich	E set domains	E-set domains of sugar-utilizing enzymes	Galactose oxidase, C-terminal domain	(Hypomyces rosellus ) [TaxId: 5132 ],	SCOPe (2.08)
A	d1goga2	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	Galactose-binding domain	Galactose oxidase, N-terminal domain	(Hypomyces rosellus ) [TaxId: 5132 ],	SCOPe (2.08)
A	d1goga3	All beta proteins	7-bladed beta-propeller	Galactose oxidase, central domain	Galactose oxidase, central domain	Galactose oxidase, central domain	(Hypomyces rosellus ) [TaxId: 5132 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Galactose oxidase, central domain	8042844	3001660	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	galactose-binding domain-like	8041133	3000087	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	E set domains	8054887	3000070	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	F5_F8_type_C_1	e1gogA1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: F5_F8_type_C_1	ECOD (1.6)
A	DUF1929	e1gogA2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: DUF1929	ECOD (1.6)
A	Glyoxal_oxid_N	e1gogA3	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: Glyoxal_oxid_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
A	2.130.10.80	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
A	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00754	F5/8 type C domain (F5_F8_type_C)	F5/8 type C domain	This domain is also known as the discoidin (DS) domain family [1].	Domain
A	PF09118	Galactose oxidase-like, Early set domain (GO-like_E_set)	Galactose oxidase-like, Early set domain	E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol subs ...	E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology [1]. This domain is found in sugar-utilising enzymes, such as galactose oxidase or chitinase [2-6].	Domain
A	PF01344	Kelch motif (Kelch_1)	Kelch motif	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	GALACTOSE OXIDASE	oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor oxidoreductase activity galactose oxidase activity oxidoreductase activity, acting on CH-OH group of donors catalytic activity cation binding ion binding binding metal ion binding small molecule binding	-	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000421	Coagulation factor 5/8, C-terminal domain	Domain
A	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A	IPR015202	Galactose oxidase-like, Early set domain	Domain
A	IPR014756	Immunoglobulin E-set	Homologous Superfamily
A	IPR037293	Galactose oxidase, central domain superfamily	Homologous Superfamily
A	IPR006652	Kelch repeat type 1	Repeat
A	IPR011043	Galactose oxidase/kelch, beta-propeller	Homologous Superfamily
A	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	galactose oxidiase M-CSA #322	Galactose oxidase is a copper containing enzyme which oxidises primary alcohols to aldehydes by the reduction of molecular oxygen to hydrogen peroxide. The enzyme catalyses the oxidation of many substrates, including dihydroxyacetone, small molecules and olysaccharides by use of a protein radical cofactor, a novel metalloradical complex, formed by a unique structural feature at the copper site with a novel thioether bond linking Cys 228 and Tyr 272 formed from a post-translational modification, which is in a stacking interaction with Trp 290. Galactose oxidase is remarkable in the extent to which free radicals are involved in all aspects of the enzyme function: serving as a key feature of the active site structure, defining the characteristic reactivity of the complex, and directing the biogenesis of the Tyr-Cys cofactor during protein maturation.	Defined by 6 residues: CYS:A-228TYR:A-272TRP:A-290TYR:A-495HIS:A-496HIS:A-581 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.1.3.9 (PDB Primary Data) Search M-CSA Motif + EC 1.1.3.9

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.