Structure of PDB 1dgm Chain A

Receptor sequence
>1dgmA (length=346) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
TGPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLD
QFNPTSLPGGSALNSVRVVQKLLRKPGSAGYMGAIGDDPRGQVLKELCDK
EGLATRFMVAPGQSTGVCAVLINEKERTLCTHLGACGSFRLPEDWTTFAS
GALIFYATAYTLTATPKNAFEVAGYAHGIPNAIFTLNLSAPFCVELYKDA
MQSLLLHTNILFGNEEEFAHLAKVHNLVTANKEHAVEVCTGALRLLTAGQ
NTGATKLVVMTRGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAG
DAFVGGFLYALSQGKTVKQCIMCGNACAQDVIQHVGFSLSFTSLPC
3D structure
PDB1dgm Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution.
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) R136 G315 A316 G317 D318
Catalytic site (residue number reindexed from 1) R127 G298 A299 G300 D301
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 MG A A185 I188 A191 A176 I179 A182
BS02 ADN A N20 D24 G69 S70 Y169 D318 N11 D15 G60 S61 Y160 D301 PDBbind-CN: -logKd/Ki=5.05,Ki=8.9uM
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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Cellular Component
External links
PDB RCSB:1dgm, PDBe:1dgm, PDBj:1dgm
PDBsum1dgm
PubMed10794412
UniProtQ9TVW2|ADK_TOXGO Adenosine kinase (Gene Name=AK)

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