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1GLV

THREE-DIMENSIONAL STRUCTURE OF THE GLUTATHIONE SYNTHETASE FROM ESCHERICHIA COLI B AT 2.0 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004363molecular_functionglutathione synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006750biological_processglutathione biosynthetic process
A0016874molecular_functionligase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATRP151
AGLU294
AGLU296

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gsa
ChainResidueDetails
AARG225
ALYS160
AARG210

site_idMCSA1
Number of Residues7
DetailsM-CSA 199
ChainResidueDetails
ALYS125electrostatic stabiliser
ALYS160electrostatic stabiliser, hydrogen bond donor
AARG210electrostatic stabiliser, hydrogen bond donor
AARG225electrostatic stabiliser, hydrogen bond donor
AASP273metal ligand
AGLU281metal ligand
AASN283metal ligand

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PDB entries from 2025-06-18

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