Structure of PDB 3d2d Chain A

Receptor sequence

>3d2dA (length=500) Species: 3467 (Eschscholzia californica)

AEAGNDLLSCLTFNGVRNHTVFSADSDSDFNRFLHLSIQNPLFQNSLISK
PSAIILPGSKEELSNTIRCIRKGSWTIRLRSGGHSYEGLSYTSDTPFILI
DLMNLNRVSIDLESETAWVESGSTLGELYYAITESSSKLGFTAGWCPTVG
TGGHISGGGFGMMSRKYGLAADNVVDAILIDANGAILDRQAMGEDVFWAI
RGGGGGVWGAIYAWKIKLLPVPEKVTVFRVTKNVAIDEATSLLHKWQFVA
EELEEDFTLSVLGGADEKQVWLTMLGFHFGLKTVAKSTFDLLFPELGLVE
EDYLEMSWGESFAYLAGLETVSQLNNRFLKFDERAFKTKVDLTKEPLPSK
AFYGLLERLSKEPNGFIALNGFGGQMSKISSDFTPFPHRSGTRLMVEYIV
AWNQSEQKKKTEFLDWLEKVYEFMKPFVSKNPRLGYVNHIDLDLGGIDWG
NKTVVNNAIEISRSWGESYFLSNYERLIRAKTLIDPNNVFNHPQSIPPMA

3D structure

• PDB: 3d2d A concerted mechanism for berberine bridge enzyme
• Chain: A
• Resolution: 2.796 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	FAD	A	L99 R100 S101 G102 G103 H104 S105 Y106 S110 L122 S141 W165 C166 V169 G170 G173 H174 G225 G226 I231 Y456 N458 H459	L79 R80 S81 G82 G83 H84 S85 Y86 S90 L102 S121 W145 C146 V149 G150 G153 H154 G205 G206 I211 Y436 N438 H439
BS02	REN	A	Y106 W165 L282 D352 F356 A388 N390 E417	Y86 W145 L262 D332 F336 A368 N370 E397

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:3d2d, PDBe:3d2d, PDBj:3d2d
• PDBsum: 3d2d
• PubMed: 18953357
• UniProt: P30986|RETO_ESCCA Reticuline oxidase (Gene Name=BBE1)