Structure of PDB 5vsa Chain C

Receptor sequence
>5vsaC (length=310) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MRIPLVGKDSIESKDIGFTLIHEHLRVFSEAVRQQWPHLYNEDEEFRNAV
NEVKRAMQFGVKTIVDPTVMGLGRDIRFMEKVVKATGINLVAGTGIYIYI
DLPFYFLNRSIDEIADLFIHDIKEGIQGTLNKAGFVKIAADEPGITKDVE
KVIRAAAIANKETKVPIITHSNAHNNTGLEQQRILTEEGVDPGKILIGHL
GDTDNIDYIKKIADKGSFIGLDRYGLDLFLPVDKRNETTLRLIKDGYSDK
IMISHDYLCTFDAPEYKPKLAPRWSITLIFEDTIPFLKRNGVNEEVIATI
FKENPKKFFS
3D structure
PDB5vsa Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.
ChainC
Resolution2.0 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 C H22 H24 K137 D256 H22 H24 K137 D256
BS02 CO C K137 H170 H199 K137 H170 H199
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:5vsa, PDBe:5vsa, PDBj:5vsa
PDBsum5vsa
PubMed29196634
UniProtQ97VT7|PHP_SACS2 Aryldialkylphosphatase (Gene Name=php)

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