Structure of PDB 1lik Chain A

Receptor sequence
>1likA (length=330) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
GPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLDQ
FNPTSLPGGSALNSVRVVQKLLRKPGSAGYMGAIGDDPRGQVLKELCDKE
GLATRFMVAPGQSTGTCAVLINEKERTLCTHLGACGSFRIPENWTTFASG
ALIFYATAYTLTATPKNALEVAGYAHGIPNAIFTLNLSAPFCVELYKDAM
QSLLLHTNILFGNEEEFAHLAKVHNLVKVALSVANKEHAVTGATKLVVMT
RGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAGDAFVGGFLYGL
SQGKTVKQCIMCGNACAQDVIQHVGFSLSF
3D structure
PDB1lik Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R136 D318
Catalytic site (residue number reindexed from 1) R126 D290
Enzyme Commision number 2.7.1.20: adenosine 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 ADN A N20 D24 G68 G69 S70 T140 Y169 D318 N10 D14 G58 G59 S60 T130 Y159 D290 BindingDB: Ki=8900nM
BS02 ADN A G280 H281 V302 N342 A345 Q346 G252 H253 V274 N314 A317 Q318 BindingDB: Ki=8900nM
Gene Ontology
Molecular Function
GO:0004001 adenosine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0006144 purine nucleobase metabolic process
GO:0006166 purine ribonucleoside salvage
GO:0016310 phosphorylation
GO:0034654 nucleobase-containing compound biosynthetic process
GO:0044209 AMP salvage
GO:0055086 nucleobase-containing small molecule metabolic process
Cellular Component
GO:0005634 nucleus
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lik, PDBe:1lik, PDBj:1lik
PDBsum1lik
PubMed10801355
UniProtQ9TVW2|ADK_TOXGO Adenosine kinase (Gene Name=AK)

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