Structure of PDB 2vc7 Chain D

Receptor sequence
>2vc7D (length=314) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MRIPLVGKDSIESKDIGFTLIHEHLRVFSEAVRQQWPHLYNEDEEFRNAV
NEVKRAMQFGVKTIVDPTVMGLGRDIRFMEKVVKATGINLVAGTGIYIYI
DLPFYFLNRSIDEIADLFIHDIKEGIQGTLNKAGFVKIAADEPGITKDVE
KVIRAAAIANKETKVPIITHSNAHNNTGLEQQRILTEEGVDPGKILIGHL
GDTDNIDYIKKIADKGSFIGLDRYGLDLFLPVDKRNETTLRLIKDGYSDK
IMISHDYCCTIDWGTAKPEYKPKLAPRWSITLIFEDTIPFLKRNGVNEEV
IATIFKENPKKFFS
3D structure
PDB2vc7 Structural Basis for Natural Lactonase and Promiscuous Phosphotriesterase Activities.
ChainD
Resolution2.05 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 HT5 D V27 L72 Y97 H170 L226 C258 I261 A266 V27 L72 Y97 H170 L226 C258 I261 A266 MOAD: Ki=432.7uM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2vc7, PDBe:2vc7, PDBj:2vc7
PDBsum2vc7
PubMed18486146
UniProtQ97VT7|PHP_SACS2 Aryldialkylphosphatase (Gene Name=php)

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