Structure of PDB 8sfb Chain D Binding Site BS02

Receptor Information
>8sfb Chain D (length=314) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRIPLVGKDSIESKDIGFTLIHEHLRGFSEAVRQQWPHLYNEDEEFRNAV
NEVKRAMQFGVKTIVDPTVMGCGRDIRFMEKVVKATGINLVAGTGIIIFI
DLPFYFLNRSIDEIADLFIHDIKEGIQGTLNKAGFVKIAADEPGITKDVE
KVIKAAAIANKETKVPIITHSNAHNNTGLEQQRILTEEGVDPGKILIGHL
GDTDNIDYIKKIADKGSFIGLDRYGLDLFLPVDKRNETTLRLIKDGYSDK
IMISHDYCCTIDWGTAKPEYKPKLAPRWSITLIFEDTIPFLKRNGVNEEV
IATIFKENPKKFFS
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain8sfb Chain D Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8sfb Changes in Active Site Loops Conformation Relates to a Transition from Lactonase to Phosphotriesterase
Resolution1.4 Å
Binding residue
(original residue number in PDB)
K137 H170 H199
Binding residue
(residue number reindexed from 1)
K137 H170 H199
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.8.1: aryldialkylphosphatase.
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:8sfb, PDBe:8sfb, PDBj:8sfb
PDBsum8sfb
PubMed
UniProtQ97VT7|PHP_SACS2 Aryldialkylphosphatase (Gene Name=php)

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