Structure of PDB 3kal Chain B

Receptor sequence

>3kalB (length=468) Species: 3847 (Glycine max)

APPLFDYHRIDQKLLQNIVYDALVWSTLNCLLVGDKSVQRSGRVPGVGLV
HLPLSLLPGPFPESHWKQGCELAPIFNELVDRVSLDGKFLQESLSRTKNA
DEFTSRLLDIHSKMLQINKKEDIRMGIVRSDYMIDEKTKSLLQIEMNTIS
TSFALIGCLMTGLHKSLLSQYGKFLGLNSNRVPANNAVDQSAEALAKAWS
EYNNPRAAILVVVQVEERNMYEQHYISALLREKHHIRSIRKTLTEIDQEG
KILPDGTLSVDGQAISVVYFRAGYTPKDYPSESEWRARLLMEQSSAIKCP
TISYHLVGTKKIQQELAKPGVLERFVENKDHIAKLRACFAGLWSLEDSDI
VKKAIENPELFVMKPQREGGGNNIYGDELRETLLKEDAAYILMQRIFPAT
SPAILVRDGNWDTGHVISEAGIFGTYLRNKDKIIINNESGYMVRTKISSS
YEGGVLPGFGVVDTVYLT

3D structure

• PDB: 3kal Structural Basis for Evolution of Product Diversity in Soybean Glutathione Biosynthesis.
• Chain: B
• Resolution: 1.9 Å

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 R444
• 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	ADP	B	I168 E169 K334 V386 K388 E392 G393 G394 N397 Y399 M424 I427 E450 K477	I144 E145 K310 V362 K364 E368 G369 G370 N373 Y375 M393 I396 E419 K446
BS02	HGS	B	R153 I173 S174 T175 S176 F177 Q238 E241 R295 Y298 R475 G485 V486	R129 I149 S150 T151 S152 F153 Q214 E217 R271 Y274 R444 G454 V455
BS03	MG	B	E169 N171 E392	E145 N147 E368
BS04	SO4	B	R153 E169 N171 G393	R129 E145 N147 G369
BS05	HGS	B	W49 N53 C182 L183	W25 N29 C158 L159

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