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1LM1

Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0006537biological_processglutamate biosynthetic process
A0006541biological_processglutamine metabolic process
A0015930molecular_functionglutamate synthase activity
A0016040molecular_functionglutamate synthase (NADH) activity
A0016041molecular_functionglutamate synthase (ferredoxin) activity
A0016491molecular_functionoxidoreductase activity
A0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
A0019676biological_processammonia assimilation cycle
A0046872molecular_functionmetal ion binding
A0051538molecular_function3 iron, 4 sulfur cluster binding
A0097054biological_processL-glutamate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT A 2074
ChainResidue
AALA879
AGLN969
ALYS972
AGLN978
ATHR1065
AGLY1066
AFMN2070
AACT2075

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 2075
ChainResidue
AGLU903
AGLN978
AARG992
AACT2074
ASER876

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN A 2070
ChainResidue
AGLY874
AMET875
ASER876
AGLY902
AGLU903
AGLN944
ALYS966
AGLN969
ALYS1034
AGLY1063
AGLY1064
ATHR1065
AGLY1066
AASP1105
AGLY1107
AGLY1128
ASER1129
AMET1132
AACT2074

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE F3S A 2072
ChainResidue
ACYS1137
AILE1138
AALA1140
AARG1141
AVAL1142
ACYS1143
ACYS1148
AVAL1152
AALA1153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For GATase activity => ECO:0000250
ChainResidueDetails
ACYS1

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS1137
ACYS1143
ACYS1148

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1jxa
ChainResidueDetails
ATYR659

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jxa
ChainResidueDetails
ALYS972
AGLU903
ACYS1

site_idMCSA1
Number of Residues9
DetailsM-CSA 111
ChainResidueDetails
ACYS1covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG31activator, electrostatic stabiliser, hydrogen bond acceptor
APHE207electrostatic stabiliser, hydrogen bond donor
AASN227electrostatic stabiliser, hydrogen bond donor
AGLY228electrostatic stabiliser, hydrogen bond donor
AGLU903electrostatic stabiliser, hydrogen bond acceptor
AGLN969electrostatic stabiliser, hydrogen bond acceptor
ALYS972activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLN978activator, hydrogen bond donor

223532

PDB entries from 2024-08-07

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