Structure of PDB 2bvg Chain C

Receptor sequence

>2bvgC (length=453) Species: 29320 (Paenarthrobacter nicotinovorans)

KLATPLSIQGEVIYPDDSGFDAIANIWDGRHLQRPSLIARCLSAGDVAKS
VRYACDNGLEISVRSGGHNPNGYATNDGGIVLDLRLMNSIHIDTAGSRAR
IGGGVISGDLVKEAAKFGLAAVTGMHPKVGFCGLALNGGVGFLTPKYGLA
SDNILGATLVTATGDVIYCSDDERPELFWAVRGAGPNFGVVTEVEVQLYE
LPRKMLAGFITWAPSVSELAGLLTSLLDALNEMADHIYPSVFVGVDENRA
PSVTVCVGHLGGLDIAERDIARLRGLGRTVSDSIAVRSYDEVVALNAEVG
SFEDGMSNLWIDREIAMPNARFAEAIAGNLDKFVSEPASGGSVKLEIEGM
PFGNPKRTPARHRDAMGVLALAEWSGAAPGSEKYPELARELDAALLRAGV
TTSGFGLLNNNSEVTAEMVAEVYKPEVYSRLAAVKREYDPENRFRHNYNI
DPE

3D structure

• PDB: 2bvg Crystal Structure of 6-Hydroxy-D-Nicotine Oxidase from Arthrobacter Nicotinovorans.
• Chain: C
• Resolution: 3.18 Å

Enzymatic activity

• Enzyme Commision number: 1.5.3.6: (R)-6-hydroxynicotine 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	C	W31 V67 S69 G70 G71 H72 N73 Y77 L88 G107 H130 V133 G134 C136 G137 G143 V144 V195 N413 N451	W27 V63 S65 G66 G67 H68 N69 Y73 L84 G103 H126 V129 G130 C132 G133 G139 V140 V191 N409 N447

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003824 catalytic activity
• GO:0016491 oxidoreductase activity
• GO:0018530 (R)-6-hydroxynicotine oxidase activity
• GO:0050660 flavin adenine dinucleotide binding
• GO:0071949 FAD binding

Biological Process

• GO:0009820 alkaloid metabolic process
• GO:0019608 nicotine catabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2bvg, PDBe:2bvg, PDBj:2bvg
• PDBsum: 2bvg
• PubMed: 16095622
• UniProt: P08159|HDNO_PAENI (R)-6-hydroxynicotine oxidase (Gene Name=6-hdno)