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3KAK

Structure of homoglutathione synthetase from Glycine max in open conformation with gamma-glutamyl-cysteine bound.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004363molecular_functionglutathione synthase activity
A0005524molecular_functionATP binding
A0006750biological_processglutathione biosynthetic process
A0009507cellular_componentchloroplast
A0016874molecular_functionligase activity
A0043295molecular_functionglutathione binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004363molecular_functionglutathione synthase activity
B0005524molecular_functionATP binding
B0006750biological_processglutathione biosynthetic process
B0009507cellular_componentchloroplast
B0016874molecular_functionligase activity
B0043295molecular_functionglutathione binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 3GC A 501
ChainResidue
AARG153
ATYR298
AILE173
ASER174
ATHR175
ASER176
AGLN238
AGLU241
AASN243
AARG295

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3GC B 501
ChainResidue
BARG153
BSER174
BSER176
BGLN238
BGLU241
BASN243
BARG295
BTYR298

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 3GC B 502
ChainResidue
BTRP90
BLYS91
BCYS94
BPRO207
BALA208
BGLU469

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2hgs
ChainResidueDetails
AARG475
AARG153
ASER176

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 2hgs
ChainResidueDetails
BARG475
BARG153
BSER176

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PDB entries from 2026-01-14

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