Structure of PDB 3l68 Chain A

Receptor sequence
>3l68A (length=358) Species: 303 (Pseudomonas putida) [Search protein sequence]
ALFEPYTLKDVTLRNRIAIPPMSQYMAEDGMINDWHHVHLAGLARGGAGL
LVVEATAVAPEGRITPGCAGIWSDAHAQAFVPVVQAIKAAGSVPGIQIAH
AGRKASANRPWEGDDHIAADDTRGWETIAPSAIAFGAHLPKVPREMTLDD
IARVKQDFVDAARRARDAGFEWIELHFAHGYLGQSFFSEHSNKRTDAYGG
SFDNRSRFLLETLAAVREVWPENLPLTARFGVLEYDGRDEQTLEESIELA
RRFKAGGLDLLSVSVGFTIPDTNIPWGPAFMGPIAERVRREAKLPVTSAW
GFGTPQLAEAALQANQLDLVSVGRAHLADPHWAYFAAKELGVEKASWTLP
APYAHWLE
3D structure
PDB3l68 Cysteine as a modulator residue in the active site of xenobiotic reductase A: a structural, thermodynamic and kinetic study
ChainA
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S25 H178 H181 Y183 R231 R240
Catalytic site (residue number reindexed from 1) S23 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 BU3 A H181 W302 H179 W300
BS02 COU A Y27 H178 H181 Y183 Y25 H176 H179 Y181 MOAD: Kd=69.2uM
BS03 FMN A P22 P23 M24 S25 A57 Q99 H178 H181 R231 A301 W302 G325 R326 P20 P21 M22 S23 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:3l68, PDBe:3l68, PDBj:3l68
PDBsum3l68
PubMed20206186
UniProtQ3ZDM6

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