Structure of PDB 2vou Chain A

Receptor sequence
>2vouA (length=393) Species: 29320 (Paenarthrobacter nicotinovorans) [Search protein sequence]
SPTTDRIAVVGGSISGLTAALMLRDAGVDVDVYERSPQPLSGFGTGIVVQ
PELVHYLLEQGVELDSISVPSSSMEYVDALTGERVGSVPADWRFTSYDSI
YGGLYELFGPERYHTSKCLVGLSQDSETVQMRFSDGTKAEANWVIGADGG
ASVVRKRLLGIEPTYAGYVTWRGVLQPGEVADDVWNYFNDKFTYGLLDDG
HLIAYPIPGRENAESPRLNFQWYWNVAEGPDLDELMTDVRGIRLPTSVHN
NSLNPHNLRQFHSKGESLFKPFRDLVLNASSPFVTVVADATVDRMVHGRV
LLIGDAAVTPRPHAAAGGAKASDDARTLAEVFTKNHDLRGSLQSWETRQL
QQGHAYLNKVKKMASRLQHGGSFEPGNPAFAFGLPKVDEPSVV
3D structure
PDB2vou Structure of 2,6-Dihydroxypyridine 3-Hydroxylase from a Nicotine-Degrading Pathway.
ChainA
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.13.10: 2,6-dihydroxypyridine 3-monooxygenase.
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 S14 I15 S16 E35 R36 I48 V49 C119 L120 D149 G150 R173 Q222 G305 D306 A316 A317 G318 G319 S13 I14 S15 E34 R35 I47 V48 C118 L119 D148 G149 R172 Q221 G304 D305 A315 A316 G317 G318
BS02 GOL A Y206 Q222 Y224 P313 Y205 Q221 Y223 P312
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0018663 2,6-dihydroxypyridine 3-monooxygenase activity
GO:0042803 protein homodimerization activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0019608 nicotine catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2vou, PDBe:2vou, PDBj:2vou
PDBsum2vou
PubMed18440023
UniProtQ93NG3|DHPH_PAENI 2,6-dihydroxypyridine 3-monooxygenase (Gene Name=dhpH)

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