Structure of PDB 3kal Chain A Binding Site BS04

Receptor Information

>3kal Chain A (length=470) Species: 3847 (Glycine max)

APPLFDYHRIDQKLLQNIVYDALVWSTLNCLLVGDKSVQRSGRVPGVGLV
HLPLSLLPGPFPESHWKQGCELAPIFNELVDRVSLDGKFLQESLSRTKNA
DEFTSRLLDIHSKMLQINKKEDIRMGIVRSDYMIDEKTKSLLQIEMNTIS
TSFALIGCLMTGLHKSLLSQYGKFLGLNSNRVPANNAVDQSAEALAKAWS
EYNNPRAAILVVVQVEERNMYEQHYISALLREKHHIRSIRKTLTEIDQEG
KILPDGTLSVDGQAISVVYFRAGYTPKDYPSESEWRARLLMEQSSAIKCP
TISYHLVGTKKIQQELAKPGVLERFVENKDHIAKLRACFAGLWSLEDSDI
VKKAIENPELFVMKPQREGGGNNIYGDELRETLLKLQEDAAYILMQRIFP
ATSPAILVRDGNWDTGHVISEAGIFGTYLRNKDKIIINNESGYMVRTKIS
SSYEGGVLPGFGVVDTVYLT

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: 3kal Chain A Residue 504

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3kal Structural Basis for Evolution of Product Diversity in Soybean Glutathione Biosynthesis.
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): M170 G332 E392
• Binding residue (residue number reindexed from 1): M146 G308 E368
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): R153 E169 N171 S176 K334 K388 E392 G393 R475
• Catalytic site (residue number reindexed from 1): R129 E145 N147 S152 K310 K364 E368 G369 R446
• Enzyme Commision number: 6.3.2.3: glutathione synthase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004363 glutathione synthase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0043295 glutathione binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006750 glutathione biosynthetic process

External links

• PDB: RCSB:3kal, PDBe:3kal, PDBj:3kal
• PDBsum: 3kal
• PubMed: 19948790
• UniProt: Q9M426