Structure of PDB 5e3t Chain A

Receptor sequence
>5e3tA (length=302) Species: 7955 (Danio rerio) [Search protein sequence]
TTSSALKGAIQLGITHSVGSLSQKPERDVLMQDFEVVESIFFPSQGSSST
PGHHHGDFKFKTYAPIAFRYFREMFGIRPDDYLYSLCNEPLIELSNGSLF
YVSSDDEFIIKTVQHKEAEFLQTLLPGYFMNLNQNMRTLLPKFYGLYCVQ
ADGKNIRIVVMNNLLPRAVPMHLKFDLKGSTYKRRASPKERSKGVPTYKD
LDFMQDMPEGILLENDHYTALSRTMQRDCRVLQSFKIMDYSLLVGIHILH
MGGIPAFNSKGERLLVFIGIIDILQSYRSVHRPSFYADRFQKFMCSTVFR
KS
3D structure
PDB5e3t Mechanism of substrate specificity of phosphatidylinositol phosphate kinases.
ChainA
Resolution3.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K171 D299
Catalytic site (residue number reindexed from 1) K111 D239
Enzyme Commision number 2.7.1.68: 1-phosphatidylinositol-4-phosphate 5-kinase.
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 ANP A F160 I169 K171 N223 L224 D236 D299 L303 D378 F100 I109 K111 N163 L164 D176 D239 L243 D272
BS02 MN A D299 D378 D239 D272
BS03 MN A D299 D378 D239 D272
Gene Ontology
Molecular Function
GO:0052742 phosphatidylinositol kinase activity
Biological Process
GO:0046488 phosphatidylinositol metabolic process

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:5e3t, PDBe:5e3t, PDBj:5e3t
PDBsum5e3t
PubMed27439870
UniProtQ503I3

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