4XAE

Structure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thaliana

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009699	biological_process	phenylpropanoid biosynthetic process
A	0009805	biological_process	coumarin biosynthetic process
A	0010421	biological_process	hydrogen peroxide-mediated programmed cell death
A	0010447	biological_process	response to acidic pH
A	0010494	cellular_component	cytoplasmic stress granule
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	1990641	biological_process	response to iron ion starvation
B	0009699	biological_process	phenylpropanoid biosynthetic process
B	0009805	biological_process	coumarin biosynthetic process
B	0010421	biological_process	hydrogen peroxide-mediated programmed cell death
B	0010447	biological_process	response to acidic pH
B	0010494	cellular_component	cytoplasmic stress granule
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0051213	molecular_function	dioxygenase activity
B	1990641	biological_process	response to iron ion starvation

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue NA A 400

Chain	Residue
A	HIS235
A	ASP237
A	HIS293

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site_id	AC2
Number of Residues	3
Details	binding site for residue NA B 400

Chain	Residue
B	HIS235
B	ASP237
B	HIS293

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"D4N500","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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