3D2D

Structure of berberine bridge enzyme in complex with (S)-reticuline

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009820	biological_process	alkaloid metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0031410	cellular_component	cytoplasmic vesicle
A	0050468	molecular_function	reticuline oxidase activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0071949	molecular_function	FAD binding

Functional Information from PROSITE/UniProt

site_id	PS00862
Number of Residues	34
Details	OX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PsaiilpgSkeELsntIrcirkgswt...IrlrSGGH

Chain	Residue	Details
A	PRO71-HIS104

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16728404, ECO:0000269|PubMed:19457868

Chain	Residue	Details
A	ASN38

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site_id	SWS_FT_FI2
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN423

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19457868

Chain	Residue	Details
A	ASN471

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CROSSLNK: 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys) => ECO:0000269|PubMed:16728404, ECO:0000269|PubMed:19457868

Chain	Residue	Details
A	HIS104
A	CYS166

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