Structure of PDB 3d2j Chain A

Receptor sequence

>3d2jA (length=502) Species: 3467 (Eschscholzia californica)

AGNDLLSCLTFNGVRNHTVFSADSDSDFNRFLHLSIQNPLFQNSLISKPS
AIILPGSKEELSNTIRCIRKGSWTIRLRSGGHSYEGLSYTSDTPFILIDL
MNLNRVSIDLESETAWVESGSTLGELYYAITESSSKLGFTAGWCPTVGTG
GHISGGGFGMMSRKYGLAADNVVDAILIDANGAILDRQAMGEDVFWAIRG
GGGGVWGAIYAWKIKLLPVPEKVTVFRVTKNVAIDEATSLLHKWQFVAEE
LEEDFTLSVLGGADEKQVWLTMLGFHFGLKTVAKSTFDLLFPELGLVEED
YLEMSWGESFAYLAGLETVSQLNNRFLKFDERAFKTKVDLTKEPLPSKAF
YGLLERLSKEPNGFIALNGFGGQMSKISSDFTPFPHRSGTRLMVEYIVAW
NQSEQKKKTEFLDWLEKVYEFMKPFVSKNPRLGYVNHIDLDLGGIDWGNK
TVVNNAIEISRSWGESYFLSNYERLIRAKTLIDPNNVFNHPQSIPPMANF
DY

3D structure

• PDB: 3d2j A concerted mechanism for berberine bridge enzyme
• Chain: A
• Resolution: 2.05 Å

Enzymatic activity

• Enzyme Commision number: 1.21.3.3: reticuline oxidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	MG	A	D45 D47	D23 D25
BS02	FAD	A	L99 R100 S101 G102 G103 H104 S105 Y106 S110 S141 G164 W165 C166 V169 G170 G172 G173 H174 F180 G225 G226 A230 I231 Y456 N458	L77 R78 S79 G80 G81 H82 S83 Y84 S88 S119 G142 W143 C144 V147 G148 G150 G151 H152 F158 G203 G204 A208 I209 Y434 N436

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity
• GO:0050468 reticuline oxidase activity
• GO:0050660 flavin adenine dinucleotide binding
• GO:0071949 FAD binding

Biological Process

• GO:0009820 alkaloid metabolic process

Cellular Component

• GO:0031410 cytoplasmic vesicle

External links

• PDB: RCSB:3d2j, PDBe:3d2j, PDBj:3d2j
• PDBsum: 3d2j
• PubMed: 18953357
• UniProt: P30986|RETO_ESCCA Reticuline oxidase (Gene Name=BBE1)