5JRO

The crystal structure of azoreductase from Yersinia pestis CO92 in its Apo form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006979	biological_process	response to oxidative stress
A	0009055	molecular_function	electron transfer activity
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0016652	molecular_function	oxidoreductase activity, acting on NAD(P)H as acceptor
A	0016655	molecular_function	oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
B	0006979	biological_process	response to oxidative stress
B	0009055	molecular_function	electron transfer activity
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0016652	molecular_function	oxidoreductase activity, acting on NAD(P)H as acceptor
B	0016655	molecular_function	oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue GOL A 301

Chain	Residue
A	PHE99
B	PHE163

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site_id	AC2
Number of Residues	2
Details	binding site for residue GOL B 301

Chain	Residue
A	ALA189
B	PHE99

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01216","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2012","submissionDatabase":"PDB data bank","title":"The crystal structure of acyl carrier protein phosphodiesterase from Yersinia pestis CO92 in complex with FMN.","authors":["Tan K.","Gu M.","Kwon K.","Anderson W.F.","Joachimiak A."]}},{"source":"PDB","id":"4ESE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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