Structure of PDB 2h8z Chain A

Receptor sequence
>2h8zA (length=359) Species: 303 (Pseudomonas putida) [Search protein sequence]
SALFEPYTLKDVTLRNRIAIPPMCQYMAEDGMINDWHHVHLAGLARGGAG
LLVVEATAVAPEGRITPGCAGIWSDAHAQAFVPVVQAIKAAGSVPGIQIA
HAGRKASANRPWEGDDHIAADDTRGWETIAPSAIAFGAHLPKVPREMTLD
DIARVKQDFVDAARRARDAGFEWIELHFAHGYLGQSFFSEHSNKRTDAYG
GSFDNRSRFLLETLAAVREVWPENLPLTARFGVLEYDGRDEQTLEESIEL
ARRFKAGGLDLLSVSVGFTIPDTNIPWGPAFMGPIAERVRREAKLPVTSA
WGFGTPQLAEAALQANQLDLVSVGRAHLADPHWAYFAAKELGVEKASWTL
PAPYAHWLE
3D structure
PDB2h8z Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: physiological function, structure and mechanism of 8-hydroxycoumarin reduction.
ChainA
Resolution1.42 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) C24 H177 H180 Y182 R230 R239
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 P21 P22 M23 C24 A56 Q98 H177 H180 R230 A300 W301 G324 R325
BS02 8CM A Y27 I66 H178 H181 Y183 Y26 I65 H177 H180 Y182 MOAD: Kd=2.5uM
BS03 8CM A R168 V221 W222 P223 R167 V220 W221 P222 MOAD: Kd=2.5uM
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:2h8z, PDBe:2h8z, PDBj:2h8z
PDBsum2h8z
PubMed16822524
UniProtQ88NF7

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