Structure of PDB 3kak Chain A

Receptor sequence
>3kakA (length=443) Species: 3847 (Glycine max) [Search protein sequence]
PLFDYHRIDQKLLQNIVYDALVWSTLNCLLVGDKSVQRSGRVPGVGLVHL
PLSLLPGPFPESHWKQGCELAPIFNELVDRVSLDGKFLQESLSRDEFTSR
LLDIHSKMLQINKDIRMGIVRSDYMIDEKTKSLLQIEMNTISTSFALIGC
LMTGLHKSLLSQYGKFLGLNSNRVPANNAVDQSAEALAKAWSEYNNPRAA
ILVVVQVEERNMYEQHYISALLREKHHIRSIRKTLTEIDQEGKILPDGTL
SVDGQAISVVYFRAGYTPKDYPSESEWRARLLMEQSSAIKCPTISYHLVG
TKKIQQELAKPGVLERFVENKDHIAKLRACFAGLWSLEDSDIVKKAIENP
ELFVMKPQNNIYGDELRETLLKAAYILMQRIFPATSPAILVRDGNWDTGH
VISEAGIFGTYLRNKDKIIINNESGYMVRTKISFGVVDTVYLT
3D structure
PDB3kak Structural Basis for Evolution of Product Diversity in Soybean Glutathione Biosynthesis.
ChainA
Resolution2.11 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R153 E169 N171 S176 K334 K388 R475
Catalytic site (residue number reindexed from 1) R121 E137 N139 S144 K302 K356 R429
Enzyme Commision number 6.3.2.3: glutathione synthase.
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 3GC A R153 S174 T175 S176 Q238 E241 N243 R295 Y298 R121 S142 T143 S144 Q206 E209 N211 R263 Y266
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3kak, PDBe:3kak, PDBj:3kak
PDBsum3kak
PubMed19948790
UniProtQ9M426

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