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7OJM

CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE H251A VARIANT COMPLEXED WITH 2-METHYL-QUINOLIN-4(1H)-ONE UNDER NORMOXIC CONDITIONS

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0003824molecular_functioncatalytic activity
AAA0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
AAA0019439biological_processobsolete aromatic compound catabolic process
AAA0050586molecular_function3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity
AAA0051213molecular_functiondioxygenase activity
BBB0003824molecular_functioncatalytic activity
BBB0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
BBB0019439biological_processobsolete aromatic compound catabolic process
BBB0050586molecular_function3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity
BBB0051213molecular_functiondioxygenase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:16187153
ChainResidueDetails
AAAALA251
BBBALA251

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AAATRP160
BBBTRP36
BBBHIS100
BBBTRP160
AAATRP36
AAAHIS100

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Increases basicity of active site His => ECO:0000250|UniProtKB:B1MFK2
ChainResidueDetails
AAAASP126
BBBASP126

219869

PDB entries from 2024-05-15

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