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2GLT

STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0.

Replaces:  1GLT
Functional Information from GO Data
ChainGOidnamespacecontents
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
AGLU281
AASN283

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

site_idMCSA1
Number of Residues8
DetailsM-CSA 199
ChainResidueDetails
ALYS125electrostatic stabiliser
ALYS160electrostatic stabiliser, hydrogen bond donor
AARG210electrostatic stabiliser, hydrogen bond donor
AARG225electrostatic stabiliser, hydrogen bond donor
AARG233electrostatic stabiliser
AASP273metal ligand
AGLU281metal ligand
AASN283metal ligand

222036

PDB entries from 2024-07-03

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