Structure of PDB 2pyw Chain A

Receptor sequence
>2pywA (length=417) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
FEEFTPLNEKSLVDYIKSTPALSSKIGADKSDDDLVIKEVGDGNLNFVFI
VVGSSGSLVIKQALPYIRCIGESWPMTKERAYFEATTLRKHGNLSPDHVP
EVYHFDRTMALIGMRYLEPPHIILRKGLIAGIEYPFLADHMSDYMAKTLF
FTSLLYHDTTEHRRAVTEFCGNVELCRLTEQVVFSDPYRVSTFNRWTSPY
LDDDAKAVREDSALKLEIAELKSMFCERAQALIHGDLHTGSVMVTQDSTQ
VIDPEFSFYGPMGFDIGAYLGNLILAFFAQDGHATQENDRKEYKQWILRT
IEQTWNLFNKRFIALWDQNKDGPGEAYLADIYNNTEVLKFVQENYMRNLL
HDSLGFGAAKMIRRIVGVAHVEDFESIEEDKRRAICERSALEFAKMLLKE
RRKFKSIGEVVSAIQQQ
3D structure
PDB2pyw Structure of A. thaliana 5-methylthioribose kinase in complex with ADP and MTR reveals a more occluded active site than its bacterial homolog
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.1.100: S-methyl-5-thioribose 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 D255 E257 D253 E255
BS02 SR1 A N46 D238 F258 R365 N44 D236 F256 R363
BS03 ADP A D44 G45 N48 V50 V61 K63 Y118 L119 I125 M245 D255 D42 G43 N46 V48 V59 K61 Y116 L117 I123 M243 D253
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0042802 identical protein binding
GO:0046522 S-methyl-5-thioribose kinase activity
Biological Process
GO:0009086 methionine biosynthetic process
GO:0016310 phosphorylation
GO:0019509 L-methionine salvage from methylthioadenosine

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Molecular Function
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Biological Process
External links
PDB RCSB:2pyw, PDBe:2pyw, PDBj:2pyw
PDBsum2pyw
PubMed17961230
UniProtQ9C6D2|MTK_ARATH Methylthioribose kinase (Gene Name=MTK)

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