Structure of PDB 3uf9 Chain D

Receptor sequence
>3uf9D (length=314) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MRIPLVGKDSIESKDIGFTLIHEHLRVFSEAVRQQWPHLYNEDEEFRNAV
NEVKRAMQFGVKTIVDPTVMGLGRDIRFMEKVVKATGINLVAGTGIYIYI
DLPFYFLNRSIDEIADLFIHDIKEGIQGTLNKAGFVKIAADEPGITKDVE
KVIRAAAIANKETKVPIITHSNAHNNTGLEQQRILTEEGVDPGKILIGHL
GDTDNIDYIKKIADKGSFIGLDRYGLDLFLPVDKRNETTLRLIKDGYSDK
IMISHDYCCTIDWGTAKPEYKPKLAPRWSITLIFEDTIPFLKRNGVNEEV
IATIFKENPKKFFS
3D structure
PDB3uf9 Characterisation of the organophosphate hydrolase catalytic activity of SsoPox
ChainD
Resolution2.68 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H22 H24 K137 H170 H199 D202 R223 D256
Catalytic site (residue number reindexed from 1) H22 H24 K137 H170 H199 D202 R223 D256
Enzyme Commision number 3.1.8.1: aryldialkylphosphatase.
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 FE2 D H22 H24 K137 D256 H22 H24 K137 D256
BS02 CO D K137 H170 H199 K137 H170 H199
BS03 FST D H24 R223 F229 D256 C258 W263 T265 A266 W278 H24 R223 F229 D256 C258 W263 T265 A266 W278
Gene Ontology
Molecular Function
GO:0004063 aryldialkylphosphatase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3uf9, PDBe:3uf9, PDBj:3uf9
PDBsum3uf9
PubMed23139857
UniProtQ97VT7|PHP_SACS2 Aryldialkylphosphatase (Gene Name=php)

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