Structure of PDB 2h8x Chain A

Receptor sequence
>2h8xA (length=358) Species: 303 (Pseudomonas putida) [Search protein sequence]
ALFEPYTLKDVTLRNRIAIPPMCQYMAEDGMINDWHHVHLAGLARGGAGL
LVVEATAVAPEGRITPGCAGIWSDAHAQAFVPVVQAIKAAGSVPGIQIAH
AGRKASANRPWEGDDHIAADDTRGWETIAPSAIAFGAHLPKVPREMTLDD
IARVKQDFVDAARRARDAGFEWIELHFAHGYLGQSFFSEHSNKRTDAYGG
SFDNRSRFLLETLAAVREVWPENLPLTARFGVLEYDGRDEQTLEESIELA
RRFKAGGLDLLSVSVGFTIPDTNIPWGPAFMGPIAERVRREAKLPVTSAW
GFGTPQLAEAALQANQLDLVSVGRAHLADPHWAYFAAKELGVEKASWTLP
APYAHWLE
3D structure
PDB2h8x Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: physiological function, structure and mechanism of 8-hydroxycoumarin reduction.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C25 H178 H181 Y183 R231 R240
Catalytic site (residue number reindexed from 1) C23 H176 H179 Y181 R229 R238
Enzyme Commision number 1.6.99.1: NADPH dehydrogenase.
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 FMN A P22 P23 M24 C25 A57 Q99 H178 H181 R231 A301 W302 G325 R326 P20 P21 M22 C23 A55 Q97 H176 H179 R229 A299 W300 G323 R324
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003959 NADPH dehydrogenase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding

View graph for
Molecular Function
External links
PDB RCSB:2h8x, PDBe:2h8x, PDBj:2h8x
PDBsum2h8x
PubMed16822524
UniProtQ88NF7

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