Structure of PDB 2pyw Chain A Binding Site BS01

Receptor Information

>2pyw Chain A (length=417) Species: 3702 (Arabidopsis thaliana)

FEEFTPLNEKSLVDYIKSTPALSSKIGADKSDDDLVIKEVGDGNLNFVFI
VVGSSGSLVIKQALPYIRCIGESWPMTKERAYFEATTLRKHGNLSPDHVP
EVYHFDRTMALIGMRYLEPPHIILRKGLIAGIEYPFLADHMSDYMAKTLF
FTSLLYHDTTEHRRAVTEFCGNVELCRLTEQVVFSDPYRVSTFNRWTSPY
LDDDAKAVREDSALKLEIAELKSMFCERAQALIHGDLHTGSVMVTQDSTQ
VIDPEFSFYGPMGFDIGAYLGNLILAFFAQDGHATQENDRKEYKQWILRT
IEQTWNLFNKRFIALWDQNKDGPGEAYLADIYNNTEVLKFVQENYMRNLL
HDSLGFGAAKMIRRIVGVAHVEDFESIEEDKRRAICERSALEFAKMLLKE
RRKFKSIGEVVSAIQQQ

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 2pyw Chain A Residue 500

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2pyw Structure of A. thaliana 5-methylthioribose kinase in complex with ADP and MTR reveals a more occluded active site than its bacterial homolog
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): D255 E257
• Binding residue (residue number reindexed from 1): D253 E255
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.7.1.100: S-methyl-5-thioribose kinase.

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

External links

• PDB: RCSB:2pyw, PDBe:2pyw, PDBj:2pyw
• PDBsum: 2pyw
• PubMed: 17961230
• UniProt: Q9C6D2|MTK_ARATH Methylthioribose kinase (Gene Name=MTK)