Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1LLW

Structural studies on the synchronization of catalytic centers in glutamate synthase: complex with 2-oxoglutarate

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 Residues20
DetailsBINDING SITE FOR RESIDUE FMN A 2070
ChainResidue
AGLY874
AGLY1063
AGLY1064
ATHR1065
AGLY1066
AASP1105
AGLY1106
AGLY1107
AGLY1128
ASER1129
AILE1130
AMET875
AAKG2073
ASER876
AGLY902
AGLU903
AGLN944
ALYS966
AGLN969
ALYS1034

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE F3S A 2072
ChainResidue
ACYS1137
AILE1138
AALA1140
AARG1141
AVAL1142
ACYS1143
ACYS1148
AALA1153

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AKG A 2073
ChainResidue
ASER876
AALA879
AGLU903
AGLN969
ALYS972
AGLY977
AGLN978
AARG992
ATHR1065
AGLY1066
AFMN2070

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

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon