Structure of PDB 2bvh Chain A

Receptor sequence
>2bvhA (length=453) Species: 29320 (Paenarthrobacter nicotinovorans) [Search protein sequence]
KLATPLSIQGEVIYPDDSGFDAIANIWDGRHLQRPSLIARCLSAGDVAKS
VRYACDNGLEISVRSGGHNPNGYATNDGGIVLDLRLMNSIHIDTAGSRAR
IGGGVISGDLVKEAAKFGLAAVTGMHPKVGFCGLALNGGVGFLTPKYGLA
SDNILGATLVTATGDVIYCSDDERPELFWAVRGAGPNFGVVTEVEVQLYE
LPRKMLAGFITWAPSVSELAGLLTSLLDALNEMADHIYPSVFVGVDENRA
PSVTVCVGHLGGLDIAERDIARLRGLGRTVSDSIAVRSYDEVVALNAEVG
SFEDGMSNLWIDREIAMPNARFAEAIAGNLDKFVSEPASGGSVKLEIEGM
PFGNPKRTPARHRDAMGVLALAEWSGAAPGSEKYPELARELDAALLRAGV
TTSGFGLLNNNSEVTAEMVAEVYKPEVYSRLAAVKREYDPENRFRHNYNI
DPE
3D structure
PDB2bvh Crystal Structure of 6-Hydroxy-D-Nicotine Oxidase from Arthrobacter Nicotinovorans.
ChainA
Resolution2.9 Å
3D
structure
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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 A W31 V67 S69 G70 G71 H72 N73 Y77 L88 G128 H130 V133 G134 C136 G137 L138 L140 G143 V144 P190 V195 N413 N451 W27 V63 S65 G66 G67 H68 N69 Y73 L84 G124 H126 V129 G130 C132 G133 L134 L136 G139 V140 P186 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2bvh, PDBe:2bvh, PDBj:2bvh
PDBsum2bvh
PubMed16095622
UniProtP08159|HDNO_PAENI (R)-6-hydroxynicotine oxidase (Gene Name=6-hdno)

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