8ORO

CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) S101A VARIANT COMPLEXED WITH 2-METHYL-QUINOLIN-4(1H)-ONE UNDER HYPEROXYC CONDITIONS

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0009056	biological_process	catabolic process
AAA	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
AAA	0050586	molecular_function	3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity
AAA	0051213	molecular_function	dioxygenase activity
BBB	0009056	biological_process	catabolic process
BBB	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
BBB	0050586	molecular_function	3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity
BBB	0051213	molecular_function	dioxygenase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:16187153

Chain	Residue	Details
AAA	HIS251
BBB	HIS251

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
AAA	TRP36
AAA	HIS100
AAA	TRP160
BBB	TRP36
BBB	HIS100
BBB	TRP160

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Increases basicity of active site His => ECO:0000250|UniProtKB:B1MFK2

Chain	Residue	Details
AAA	ASP126
BBB	ASP126

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