Structure of PDB 1lii Chain A

Receptor sequence
>1liiA (length=331) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
GPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLDQ
FNPTSLPGGSALNSVRVVQKLLRKPGSAGYMGAIGDDPRGQVLKELCDKE
GLATRFMVAPGQSTGTCAVLINEKERTLCTHLGACGSFRIPENWTTFASG
ALIFYATAYTLTATPKNALEVAGYAHGIPNAIFTLNLSAPFCVELYKDAM
QSLLLHTNILFGNEEEFAHLAKVHNLVAKVALSVANKEHAVEGATKLVVM
TRGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAGDAFVGGFLYG
LSQGKTVKQCIMCGNACAQDVIQHVGFSLSF
3D structure
PDB1lii Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.
ChainA
Resolution1.73 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 D291
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 I22 D24 G68 G69 S70 C127 T140 Y169 N314 D318 N10 I12 D14 G58 G59 S60 C117 T130 Y159 N287 D291 BindingDB: Ki=8900nM
BS02 ACP A R136 T278 G280 H281 V302 T313 N314 G315 A316 G317 D318 N342 A345 Q346 R126 T251 G253 H254 V275 T286 N287 G288 A289 G290 D291 N315 A318 Q319
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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Cellular Component
External links
PDB RCSB:1lii, PDBe:1lii, PDBj:1lii
PDBsum1lii
PubMed10801355
UniProtQ9TVW2|ADK_TOXGO Adenosine kinase (Gene Name=AK)

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