Structure of PDB 5w3u Chain A

Receptor sequence
>5w3uA (length=293) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
RIPLVGKDSIESKDIGFTLIHEHLRAFSEAVRQQWPHLYNEDEEFRNAVN
EVKRAMQFGVKTIVDPTVMGLGRDTRFMEKVVKATGINLVAGTGIWIFID
LPFYFLNRSIDEIADLFIHDIKEGIQGTPNKAGFVKIAADEPGITKDVEK
VIRAAAIANKETKVPIITHSNAHNNTGLEQQRILTEEGVDPGKILIGHLG
DTDNIDYIKKIADKGSFIGLDRYGVDLFLPVDKRNETTLRLIKDGYSDKI
MISHDYWSITLIFEDTIPFLKRNGVNEEVIATIFKENPKKFFS
3D structure
PDB5w3u Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.
ChainA
Resolution2.5 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) H21 H23 K136 H169 H198 D201 R222 D255
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 A H22 H24 K137 D256 H21 H23 K136 D255
BS02 CO A H22 K137 H170 H199 D256 H21 K136 H169 H198 D255
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:5w3u, PDBe:5w3u, PDBj:5w3u
PDBsum5w3u
PubMed29196634
UniProtQ97VT7|PHP_SACS2 Aryldialkylphosphatase (Gene Name=php)

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