Structure of PDB 1ka0 Chain A

Receptor sequence
>1ka0A (length=353) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
LERELLVATQAVRKASLLTKRIQSEVISHKDSTTITKNDNSPVTTGDYAA
QTIIINAIKSNFPDDKVVGEESSSGLSDAFVSGILNEIKANDEVYNKNYK
KDDFLFTNDQFPLKSLEDVRQIIDFGNYEGGRKGRFWCLDPIDGTKGFLR
GEQFAVCLALIVDGVVQLGCIGCPNLVLSSYGAQDLKGHESFGYIFRAVR
GLGAFYSPSSDAESWTKIHVRHLKDTKDMITLEGVEKGHSSHDEQTAIKN
KLNISKSLHLDSQAKYCLLALGLADVYLRLPIKLSYQEKIWDHAAGNVIV
HEAGGIHTDAMEDVPLDFGNGRTLATKGVIASSGPRELHDLVVSTSCDVI
QSR
3D structure
PDB1ka0 Hal2p: Ion selectivity and implications on inhibition mechanism
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D49 E72 D142 I144 D145 T147 D294
Catalytic site (residue number reindexed from 1) D47 E70 D140 I142 D143 T145 D292
Enzyme Commision number 3.1.3.7: 3'(2'),5'-bisphosphate nucleotidase.
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 AMP A H241 D263 S264 K267 R281 Y288 D294 H239 D261 S262 K265 R279 Y286 D292
Gene Ontology
Molecular Function
GO:0008441 3'(2'),5'-bisphosphate nucleotidase activity
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0000103 sulfate assimilation
GO:0006790 sulfur compound metabolic process
GO:0009086 methionine biosynthetic process
GO:0016078 tRNA decay
GO:0042538 hyperosmotic salinity response
GO:0046854 phosphatidylinositol phosphate biosynthetic process
Cellular Component
GO:0005575 cellular_component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ka0, PDBe:1ka0, PDBj:1ka0
PDBsum1ka0
PubMed
UniProtP32179|MET22_YEAST 3'(2'),5'-bisphosphate nucleotidase (Gene Name=MET22)

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