Structure of PDB 5vrk Chain B

Receptor sequence
>5vrkB (length=314) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MRIPLVGKDSIESKDIGFTLIHEHLRVFSEAVRQQWPHLYNEDEELRNAV
NEVKRAMQFGVKTIVDPTVMGLGRDIRFMEKVVKATGINLVAGTGIYIYI
DLPFYFLNRSIDEIADLFIHDIKEGIQGTLNKAGFVKIAADEPGITKDVE
KVIRAAAIANKETKVPIITHSNAHNNTGLEQQRILTEEGVDPGKILIGHL
GDTDNIDYIKKIADKGSFIGLDRYGLDLFLPVDKRNETTLRLIKDGYSDK
IMISHDYACTIDMGTAKPEYKPKLAPRWSTTLIFEDTIPFLKRNGVNEEV
IATIFKENPKKFFS
3D structure
PDB5vrk Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.
ChainB
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B H22 H24 K137 D256 H22 H24 K137 D256
BS02 CO B 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5vrk, PDBe:5vrk, PDBj:5vrk
PDBsum5vrk
PubMed29196634
UniProtQ97VT7|PHP_SACS2 Aryldialkylphosphatase (Gene Name=php)

[Back to BioLiP]