Structure of PDB 3kal Chain A

Receptor sequence
>3kalA (length=470) Species: 3847 (Glycine max) [Search protein sequence]
APPLFDYHRIDQKLLQNIVYDALVWSTLNCLLVGDKSVQRSGRVPGVGLV
HLPLSLLPGPFPESHWKQGCELAPIFNELVDRVSLDGKFLQESLSRTKNA
DEFTSRLLDIHSKMLQINKKEDIRMGIVRSDYMIDEKTKSLLQIEMNTIS
TSFALIGCLMTGLHKSLLSQYGKFLGLNSNRVPANNAVDQSAEALAKAWS
EYNNPRAAILVVVQVEERNMYEQHYISALLREKHHIRSIRKTLTEIDQEG
KILPDGTLSVDGQAISVVYFRAGYTPKDYPSESEWRARLLMEQSSAIKCP
TISYHLVGTKKIQQELAKPGVLERFVENKDHIAKLRACFAGLWSLEDSDI
VKKAIENPELFVMKPQREGGGNNIYGDELRETLLKLQEDAAYILMQRIFP
ATSPAILVRDGNWDTGHVISEAGIFGTYLRNKDKIIINNESGYMVRTKIS
SSYEGGVLPGFGVVDTVYLT
3D structure
PDB3kal Structural Basis for Evolution of Product Diversity in Soybean Glutathione Biosynthesis.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 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.
Interaction with ligand
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3kal, PDBe:3kal, PDBj:3kal
PDBsum3kal
PubMed19948790
UniProtQ9M426

[Back to BioLiP]