Structure of PDB 1gsa Chain A

Receptor sequence
>1gsaA (length=314) Species: 37762 (Escherichia coli B) [Search protein sequence]
MIKLGIVMDPIANINIKKDSSFAMLLEAQRRGYELHYMEMGDLYLINGEA
RAHTRTLNVKQNYEEWFSFVGEQDLPLADLDVILMRKDPPFDTEFIYATY
ILERAEEKGTLIVNKPQSLRDCNEKLFTAWFSDLTPETLVTRNKAQLKAF
WEKHSDIILKPLDGMGGASIFRVKEGDPNLGVIAETLTEHGTRYCMAQNY
LPAIKDGDKRVLVVDGEPVPYCLARIPQGGETRGNLAAGGRGEPRPLTES
DWKIARQIGPTLKEKGLIFVGLDIIGDRLTEINVTSPTCIREIEAEFPVS
ITGMLMDAIEARLQ
3D structure
PDB1gsa A pseudo-michaelis quaternary complex in the reverse reaction of a ligase: structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 A resolution.
ChainA
Resolution2.0 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) K125 K160 R210 R225 R233 D273 E281 N283
Catalytic site (residue number reindexed from 1) K125 K160 R210 R225 R233 D273 E281 N283
Enzyme Commision number 6.3.2.3: glutathione synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004363 glutathione synthase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006750 glutathione biosynthetic process
GO:0051289 protein homotetramerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1gsa, PDBe:1gsa, PDBj:1gsa
PDBsum1gsa
PubMed8810901
UniProtP04425|GSHB_ECOLI Glutathione synthetase (Gene Name=gshB)

[Back to BioLiP]